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(fructosylsucrose)4 + H2O
?
-
-
-
-
?
(fructosylsucrose)5 + H2O
?
-
-
-
-
?
(fructosylsucrose)6 + H2O
?
-
-
-
-
?
(fructosylsucrose)7 + H2O
?
-
-
-
-
?
(fructosylsucrose)9 + H2O
?
-
-
-
-
?
1-kestose + H2O
?
-
-
-
-
?
1f-fructofuranosyl nystose + H2O
disaccharides + trisaccharides
-
-
-
?
agavin + H2O
?
hydrolysis of agavins from stems of Agave angustifolia, from 8-year-old plants collected in Santiago Matatlan region, Oaxaca, Mexico. Analysis of hydrolysis products from reaction of endo-inulinase and exo-inulinase (EC 3.2.1.80) on agavins, detailed overview. Complete hydrolysis of agavins from Agave angustifolia is not reached in any of the inulinase treatments employed. A mixture of 25% exo- and 75% endo-inulinase shows a positive synergistic action on agavins degradation because it significantly reduces the hydrolysis time in relation to the use of only endo-inulinase treatments
-
-
?
fructooligosaccharide + H2O
?
-
(fructosylsucrose)4 to (fructosylsucrose)9
-
-
?
inulin + H2O
1,1,1-kestopentaose + 1-kestose
inulin + H2O
1-kestose + ?
-
-
-
?
inulin + H2O
beta-D-fructose + inulobiose + fructooligosaccharides
-
-
-
-
?
inulin + H2O
D-fructose + fructo-oligosaccharides
-
-
-
-
?
inulin + H2O
inulooligofructose
inulin + H2O
inulooligosaccharide
-
-
ranging from DP2 to DP7
-
?
inulin + H2O
inulooligosaccharides
inulin + H2O
inulotetraose + inulotriose
-
enzyme produces equal amounts of inulotetraose and inulotriose
-
?
inulin + H2O
inulotriose + inulotetraose
inulin + H2O
inulotriose + inulotetraose + inulopentaose
inulin + H2O
monosaccharide + disaccharide + oligosaccharide
inulin + H2O
oligofructosides
inulin + H2O
oligosaccharides
nystose + H2O
?
-
-
-
-
?
raffinose + H2O
?
-
-
-
-
?
raffinose + H2O
D-fructose + ?
raffinose + H2O
D-fructose + D-galactopyranosyl-(1-6)-D-glucopyranoside
-
-
-
-
?
sucrose + H2O
alpha-D-glucopyranose + beta-D-fructofuranose
sucrose + H2O
beta-D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
additional information
?
-
inulin + H2O
1,1,1-kestopentaose + 1-kestose
-
thin layer chromatography analysis of reaction products formed during hydrolysis of inulin by purified endoinulinase
-
-
?
inulin + H2O
1,1,1-kestopentaose + 1-kestose
-
thin layer chromatography analysis of reaction products formed during hydrolysis of inulin by purified endoinulinase
-
-
?
inulin + H2O
?
-
-
-
?
inulin + H2O
?
-
Asp460 is a catalytic residue, presence of a carboxylate group in this position is a prerequisite for catalysis
-
-
?
inulin + H2O
?
-
-
major products of hydrolysis are fructo-oligosaccharides with degree of polymerization from 3 to 4
-
?
inulin + H2O
?
-
-
major products of hydrolysis are fructo-oligosaccharides with degree of polymerization from 3 to 4
-
?
inulin + H2O
?
-
during the hydrolysis process, at first longer saccharide chains appear, which are subsequently cut into shorter fragments
-
-
?
inulin + H2O
?
-
best substrate is inulin from chicory, followed in decreasing order by inulins from topinambur and dahlia
-
-
?
inulin + H2O
?
substrate from chicory, 23% and 85% hydrolysis at 40 and 400 U/g fructan, respectively, at pH 5.0, 30°C, in 24 h
-
-
?
inulin + H2O
?
-
during the hydrolysis process, at first longer saccharide chains appear, which are subsequently cut into shorter fragments
-
-
?
inulin + H2O
?
-
broad substrate specificity, but greater affinity for inulin substrate
-
-
?
inulin + H2O
?
-
broad substrate specificity, but greater affinity for inulin substrate
-
-
?
inulin + H2O
?
-
37°C, 15 min, pH 4.5
-
-
?
inulin + H2O
?
-
raw inulin from Asparagus officinalis
-
-
?
inulin + H2O
?
-
37°C, 15 min, pH 4.5
-
-
?
inulin + H2O
?
-
raw inulin from Asparagus officinalis
-
-
?
inulin + H2O
inulooligofructose
-
-
-
-
?
inulin + H2O
inulooligofructose
-
-
-
-
?
inulin + H2O
inulooligosaccharides
-
-
-
?
inulin + H2O
inulooligosaccharides
using inulin from Jerusalem artichoke
-
-
?
inulin + H2O
inulooligosaccharides
-
-
-
?
inulin + H2O
inulooligosaccharides
using inulin from Jerusalem artichoke
-
-
?
inulin + H2O
inulooligosaccharides
-
-
-
?
inulin + H2O
inulooligosaccharides
using inulin from Jerusalem artichoke
-
-
?
inulin + H2O
inulooligosaccharides
-
-
-
?
inulin + H2O
inulooligosaccharides
using inulin from Jerusalem artichoke
-
-
?
inulin + H2O
inulooligosaccharides
-
-
-
-
?
inulin + H2O
inulooligosaccharides
-
-
-
-
?
inulin + H2O
inulotriose + inulotetraose
the purified recombinant enzyme efficiently produces inulooligosaccharides from inulin, with inulotriose and inulotetraose as major products. When 10, 30, 50, and 100 g/l of inulin is used as substrate, the final conversion ratio of total inulooligosaccharides reaches 88.4%, 83.5%, 80.2%, and 60.1%, respectively. Carbohydrate compositions of reaction products from various concentrations of inulin substrate, overview
-
-
?
inulin + H2O
inulotriose + inulotetraose
the purified recombinant enzyme efficiently produces inulooligosaccharides from inulin, with inulotriose and inulotetraose as major products. When 10, 30, 50, and 100 g/l of inulin is used as substrate, the final conversion ratio of total inulooligosaccharides reaches 88.4%, 83.5%, 80.2%, and 60.1%, respectively. Carbohydrate compositions of reaction products from various concentrations of inulin substrate, overview
-
-
?
inulin + H2O
inulotriose + inulotetraose + inulopentaose
-
-
-
-
?
inulin + H2O
inulotriose + inulotetraose + inulopentaose
-
-
-
-
?
inulin + H2O
inulotriose + inulotetraose + inulopentaose
-
-
-
?
inulin + H2O
inulotriose + inulotetraose + inulopentaose
-
-
-
?
inulin + H2O
monosaccharide + disaccharide + oligosaccharide
hydrolysis with the crude recombinant inulinase
-
-
?
inulin + H2O
monosaccharide + disaccharide + oligosaccharide
hydrolysis with the crude recombinant inulinase
-
-
?
inulin + H2O
oligofructosides
-
-
mainly inulotriose, inulotetraose and inulopentaose
?
inulin + H2O
oligofructosides
-
-
-
?
inulin + H2O
oligofructosides
-
-
-
-
?
inulin + H2O
oligofructosides
-
-
fructose oligomers of various length
?
inulin + H2O
oligofructosides
-
-
inulotriose and inulotetraose are liberated as the main products after 24 h, prolonged reaction yields inulotriose as the main product
?
inulin + H2O
oligofructosides
-
-
inulotriose and inulotetraose are liberated as the main products after 24 h, prolonged reaction yields inulotriose as the main product
?
inulin + H2O
oligofructosides
-
-
inulotriose + inulotetraose + inulopentaose
?
inulin + H2O
oligofructosides
-
-
inulooligosaccharides, DP = 2-7
?
inulin + H2O
oligofructosides
-
-
inulotriose + inulotetraose + inulopentaose
?
inulin + H2O
oligofructosides
-
-
inulooligosaccharides, DP = 2-7
?
inulin + H2O
oligofructosides
-
-
the major products are trisaccharides, tetrasaccharides, pentasaccharides and hexasaccharides
?
inulin + H2O
oligosaccharides
-
only oligosaccharides, but no monosaccharides and disaccharides are detected
-
-
?
inulin + H2O
oligosaccharides
-
only oligosaccharides, but no monosaccharides and disaccharides are detected
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
A0A0K8L0R3
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
kestopentaose + H2O
?
-
-
-
?
raffinose + H2O
D-fructose + ?
-
-
-
-
?
raffinose + H2O
D-fructose + ?
-
-
-
-
?
sucrose + H2O
alpha-D-glucopyranose + beta-D-fructofuranose
-
-
-
-
?
sucrose + H2O
alpha-D-glucopyranose + beta-D-fructofuranose
-
-
-
-
?
sucrose + H2O
alpha-D-glucopyranose + beta-D-fructofuranose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
purified inulinase shows no detectable activity toward sucrose and little activity toward raffinose (0.8% of relative enzyme activity on inulin)
-
-
?
additional information
?
-
endo-inulinase breaks down the internal beta-(2,1) glycosidic linkages of inulin and liberates fructooligosaccharides (FOS) with degree of polymerization (DP) 3 to DP6 as major products
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
enzymatic synthesis of fructooligosaccharides (FOS) from sucrose by endo-inulinase-catalyzed transfructosylation reaction of sucrose in biphasic systems, production of FOS from sucrose by commercial inulinase from Aspergillus niger, modeling, overview. With the use of maple syrup 66°Bx-based biphasic medium, kestose, nystose, and fructosyl-nystose are all produced during the first 16 h, with a relative proportion of 78.79%, 20.34%, and 0.86%, respectively
-
-
?
additional information
?
-
no activity on commercial Erwinia levan or levan from Leuconostoc mesenteroides strain DSM 20343
-
-
?
additional information
?
-
-
purified inulinase shows no detectable activity toward sucrose and little activity toward raffinose (0.8% of relative enzyme activity on inulin)
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
the enzyme also exhibits invertase activity
-
-
?
additional information
?
-
A0A0K8L0R3
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
use of agroindustrial residues such as sugarcane bagasse, corn steep liquor, soybean bran, and molasses as substrate for solid-state fermentation or submerged fermentation
-
-
?
additional information
?
-
-
use of agroindustrial residues such as sugarcane bagasse, corn steep liquor, soybean bran, and molasses as substrate for solid-state fermentation or submerged fermentation
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
-
inulin rich substrates used are from chicory, asparagus roots, dahlia tubers, and dandelion roots
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
-
inulin rich substrates used are from chicory, asparagus roots, dahlia tubers, and dandelion roots
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
no activity with levan
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with raffinose
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
-
no activity with levan
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with raffinose
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
no activity with melizitose
-
-
?
additional information
?
-
-
no activity with levan
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with raffinose
-
-
?
additional information
?
-
-
no activity with melizitose
-
-
?
additional information
?
-
-
no activity with levan
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
-
no activity with raffinose
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
-
no activity with sucrose
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
the enzyme targets the internal beta-2,1 fructofuranosidic linkages of inulin to yield both GFn and Fm molecules (G for glucose, F for fructose, n and m indicate the number of fructose moieties)
-
-
?
additional information
?
-
-
the enzyme targets the internal beta-2,1 fructofuranosidic linkages of inulin to yield both GFn and Fm molecules (G for glucose, F for fructose, n and m indicate the number of fructose moieties)
-
-
?
additional information
?
-
the enzyme targets the internal beta-2,1 fructofuranosidic linkages of inulin to yield both GFn and Fm molecules (G for glucose, F for fructose, n and m indicate the number of fructose moieties)
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
-
the strain produces a mixture of endo- and exo-inulinases liberating oligosaccharides (1-kestose and 1-nystose) along with fructose
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
additional information
?
-
endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
A0A0K8L0R3
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 32, GH32
-
physiological function
Inulinases are a group of enzymes that catalyze the hydrolysis of the (2-1)-beta-D-fructosidic linkages in inulin. Inulinases can be further classified into the following two types of enzymes: exo-inulinases (EC 3.2.1.80) and endo-inulinases (EC 3.2.1.7). Endo-inulinases hydrolyze the internal linkages in inulin, yielding an oligofructose mixture with inulotriose, inulotetraose, and inulopentaose as the main components
physiological function
inulinases are fructofuranosyl hydrolases that target the beta-2,1 linkage of inulin and hydrolyze it into fructose, glucose and inulooligosaccharides (IOS), IOS are functioning as dietary fibers
physiological function
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Inulinases are a group of enzymes that catalyze the hydrolysis of the (2-1)-beta-D-fructosidic linkages in inulin. Inulinases can be further classified into the following two types of enzymes: exo-inulinases (EC 3.2.1.80) and endo-inulinases (EC 3.2.1.7). Endo-inulinases hydrolyze the internal linkages in inulin, yielding an oligofructose mixture with inulotriose, inulotetraose, and inulopentaose as the main components
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physiological function
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inulinases are fructofuranosyl hydrolases that target the beta-2,1 linkage of inulin and hydrolyze it into fructose, glucose and inulooligosaccharides (IOS), IOS are functioning as dietary fibers
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additional information
enzyme structure homology modeling using the structure of endoinulinase from Aspergillus ficcum (PDB ID 3RWK) as template
additional information
-
enzyme structure homology modeling using the structure of endoinulinase from Aspergillus ficcum (PDB ID 3RWK) as template
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
additional information
A0A0K8L0R3
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate. Catalytic residue is Glu34
additional information
reaction selectivity of transfructosylation vs. hydrolysis of endo-inulinase from Aspergillus niger in selected biphasic media, overview
additional information
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screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Aspergillus funigatus strain GNCC 1351 has endo- and exoinulinase activities
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Aspergillus niger strain ATCC 26011 has endo- and exoinulinase activities
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Penicillium citrinum strain MTCC 1256 has endo- and exoinulinase activities
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Penicillium rugulosum strain MTCC 3487 has endo- and exoinulinase activities
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Penicillium sp. strain NFCCI 2768 has endo- and exoinulinase activities
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Penicillium citrinum strain MTCC 1256 has endo- and exoinulinase activities
-
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Aspergillus niger strain ATCC 26011 has endo- and exoinulinase activities
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
-
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Penicillium rugulosum strain MTCC 3487 has endo- and exoinulinase activities
-
additional information
-
enzyme structure homology modeling using the structure of endoinulinase from Aspergillus ficcum (PDB ID 3RWK) as template
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling. Docking with kestopentaose substrate
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
-
additional information
-
screening of diverse fungal strains for exo- and endoinulinase and sucrase activities on different substrate sources, overview. Aspergillus funigatus strain GNCC 1351 has endo- and exoinulinase activities
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
-
additional information
-
in silico evaluation and identification of fungi capable of producing endo-inulinase enzyme, overview. The enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS). Molecular docking, and molecular dynamic simulation analyses, structure homology modeling
-
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D460A
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is totally inactive
D460E
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active to some extent. pKa of the acid/base catalyst decreases from 9.2 for the wild-type enzyme to 7.0 for the mutant
D460N
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active to some extent
E323A
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enzyme efficiency (kcat/Km) is significantly lower than that of the wild-type due to a substantial decrease in kcat, but not due to variations in Km consistent with its putative role as nucleophile catalyst
E519A
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enzyme efficiency (kcat/Km) is significantly lower than that of the wild-type due to a substantial decrease in kcat, but not due to variations in Km consistent with its putative role as acid/base catalyst
D298A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 59.7% of wild-typ activity
E43D
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 5.4% of wild-typ activity
F99A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 6.1% of wild-typ activity
I70A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 38.9% of wild-typ activity
M41A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 56.2% of wild-typ activity
N265A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 72.9% of wild-typ activity
N42G
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 7.1% of wild-typ activity
P62G
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 0.2% of wild-typ activity
Q59A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 2.2% of wild-typ activity
R175A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 0.1% of wild-typ activity
R295A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 84.6% of wild-typ activity
W67A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 2.4% of wild-typ activity
Y128H
site-directed mutagenesis, the mutation Y128H is in close proximity to the active site, it leads to modified enzyme catalytic activity with increased kcat and kcat/KM compared to untagged wild-type enzyme, while the activity of MBP-tagged wild-type enzyme is higher
Y128H/A316T/E344K/T504M
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
Y128H/E344K/T504M
site-directed mutagenesis, the mutation E344K is located on the enzyme protein surface, mutation Y128H is in close proximity to the active site. The mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
Y128H
-
site-directed mutagenesis, the mutation Y128H is in close proximity to the active site, it leads to modified enzyme catalytic activity with increased kcat and kcat/KM compared to untagged wild-type enzyme, while the activity of MBP-tagged wild-type enzyme is higher
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Y128H/A316T/E344K/T504M
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
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Y128H/E344K/T504M
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site-directed mutagenesis, the mutation E344K is located on the enzyme protein surface, mutation Y128H is in close proximity to the active site. The mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
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additional information
-
enzyme immobilization on chitin beads, half-life time of immobilized endo-inulinase in a packed-bed column reactor is 48 days
additional information
-
structural and storage and functional thermostabilization of endo-inulinase through semi-rational modification of surface accessible lysine residues by pyridoxal 5'-phosphate and ascorbate reduction, method, molecular dynamics simulation, overview
additional information
maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
additional information
-
maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
additional information
-
maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
-
additional information
-
maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
-
additional information
-
maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
-
additional information
genetic modification and optimization of endo-inulinase for the enzymatic production of oligofructose from inulin, method optimization, overview. The activity of recombinant truncated enzyme TrINU reaches 148 U/ml which is significantly higher than that of recombinant full-length enzyme INU with 115 U/ml. Improvement of the stability of TrINU via mutation of protease cleavage sites. The optimal reaction conditions for Fusarium oxysporum endo-inulinase are: NaAc-HAc buffer, pH 5.0, 2 mM Mg2+, 8% substrate, and an incubation temperature of 55°C
additional information
-
genetic modification and optimization of endo-inulinase for the enzymatic production of oligofructose from inulin, method optimization, overview. The activity of recombinant truncated enzyme TrINU reaches 148 U/ml which is significantly higher than that of recombinant full-length enzyme INU with 115 U/ml. Improvement of the stability of TrINU via mutation of protease cleavage sites. The optimal reaction conditions for Fusarium oxysporum endo-inulinase are: NaAc-HAc buffer, pH 5.0, 2 mM Mg2+, 8% substrate, and an incubation temperature of 55°C
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additional information
mutants M-30 (115.0 U/ml) and M-31 (52.6 U/ml) show improved inulinase production compared to the wild-type. Initial moisture, inoculum, amount ratio of wheat bran to rice bran, temperature, pH for the maximum inulinase production by the mutant M-30 is 60.5%, 2.5%, 0.42, 30°C and 6.50, respectively. Under the optimized conditions, 455.9 U/grams of dry substrate (gds) of inulinase activity is reached in the solid state fermentation culture of the mutant. Glucose repression on the inulinase production by the mutant M-30 is relieved in some degree compared to that in its parent strain when the added glucose concentrations in the media are higher than 2.0%
additional information
-
mutants M-30 (115.0 U/ml) and M-31 (52.6 U/ml) show improved inulinase production compared to the wild-type. Initial moisture, inoculum, amount ratio of wheat bran to rice bran, temperature, pH for the maximum inulinase production by the mutant M-30 is 60.5%, 2.5%, 0.42, 30°C and 6.50, respectively. Under the optimized conditions, 455.9 U/grams of dry substrate (gds) of inulinase activity is reached in the solid state fermentation culture of the mutant. Glucose repression on the inulinase production by the mutant M-30 is relieved in some degree compared to that in its parent strain when the added glucose concentrations in the media are higher than 2.0%
additional information
isolation of mutant M-30 with enhanced inulinase production, mutant is stable after cultivation for 20 generations. Inulin, yeast extract, NaCl, temperature, pH for maximum inulinase production by the mutant M-30 are 20.0 g/l, 5.0 g/l, 20.0 g/l, at 28°C and pH 6.5, respectively. Under the optimized conditions, 127.7 U/ml of inulinase activity is reached in the liquid culture
additional information
-
mutants M-30 (115.0 U/ml) and M-31 (52.6 U/ml) show improved inulinase production compared to the wild-type. Initial moisture, inoculum, amount ratio of wheat bran to rice bran, temperature, pH for the maximum inulinase production by the mutant M-30 is 60.5%, 2.5%, 0.42, 30°C and 6.50, respectively. Under the optimized conditions, 455.9 U/grams of dry substrate (gds) of inulinase activity is reached in the solid state fermentation culture of the mutant. Glucose repression on the inulinase production by the mutant M-30 is relieved in some degree compared to that in its parent strain when the added glucose concentrations in the media are higher than 2.0%
-
additional information
directed evolution yields variants showing up to 5fold improvements in soluble enzyme production compared to the starting point which enables high-yield production of highly purified recombinant enzyme. The distribution of the enzymatic reaction products demonstrates that after 24 h of incubation, the main product (57%) has a degree of polymerization of 3 (DP3). The MBP-fused wild-type enzyme shows increased activity compared to unaltered wild-type enzyme. The evolved endoinulinase mutant variants exhibit increased solubility and activity compared to wild-type
additional information
-
directed evolution yields variants showing up to 5fold improvements in soluble enzyme production compared to the starting point which enables high-yield production of highly purified recombinant enzyme. The distribution of the enzymatic reaction products demonstrates that after 24 h of incubation, the main product (57%) has a degree of polymerization of 3 (DP3). The MBP-fused wild-type enzyme shows increased activity compared to unaltered wild-type enzyme. The evolved endoinulinase mutant variants exhibit increased solubility and activity compared to wild-type
additional information
-
directed evolution yields variants showing up to 5fold improvements in soluble enzyme production compared to the starting point which enables high-yield production of highly purified recombinant enzyme. The distribution of the enzymatic reaction products demonstrates that after 24 h of incubation, the main product (57%) has a degree of polymerization of 3 (DP3). The MBP-fused wild-type enzyme shows increased activity compared to unaltered wild-type enzyme. The evolved endoinulinase mutant variants exhibit increased solubility and activity compared to wild-type
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food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
A0A0K8L0R3
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
food industry
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
industry
-
Bacillus smithii T7 is a new thermophilic bacterium that can highly produce endoinulinase. The higher temperature optimum and greater thermostability of Bacillus smithii T7 are the desirable features for industrial production of inulinase that shall be a potential heat-resistant enzyme candidate for commercial use and enzyme functional research
industry
-
higher inulinase activity from Kluyveromyces marxianus YS-1 is achieved by root powder extract of Asparagus officinalis. This plant material can be opted as a cheap inulin source for the production of inulinase
industry
inulinase activity (115.0 U/ml) in liquid production medium by the mutant M-30 is the highest reported so far. Inulinase produced by the mutant M-30 of the marine yeast strain has potentially for use in biotechnological fields
industry
-
inulinase produced by yeast strain CCMB 300 from the Brazilian semi-arid region has great potential to be used for inulin hydrolysis in the food industry
industry
yeasts can produce more inulinase than bacteria
industry
-
Bacillus smithii T7 is a new thermophilic bacterium that can highly produce endoinulinase. The higher temperature optimum and greater thermostability of Bacillus smithii T7 are the desirable features for industrial production of inulinase that shall be a potential heat-resistant enzyme candidate for commercial use and enzyme functional research
-
industry
-
higher inulinase activity from Kluyveromyces marxianus YS-1 is achieved by root powder extract of Asparagus officinalis. This plant material can be opted as a cheap inulin source for the production of inulinase
-
industry
-
inulinase activity (115.0 U/ml) in liquid production medium by the mutant M-30 is the highest reported so far. Inulinase produced by the mutant M-30 of the marine yeast strain has potentially for use in biotechnological fields
-
industry
-
inulinase produced by yeast strain CCMB 300 from the Brazilian semi-arid region has great potential to be used for inulin hydrolysis in the food industry
-
nutrition
-
production of oligosaccharides, which are soluble dietary fibers and/or a functional sweeteners
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
A0A0K8L0R3
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
production of oligosaccharides, which are soluble dietary fibers and/or a functional sweeteners
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
nutrition
-
the enzyme endo-inulinase hydrolyzes inulin to short chain fructooligosaccharides (FOS) that are potential prebiotics with many health promoting benefits. Production of FOS by endo-inulinase is a single step process that yields high quality FOS and excludes any further purification steps
-
synthesis
-
high-level expression in Pichia pastoris leads to production of enzyme at 286.8 U/ml and 8873 U/mg
synthesis
isolation of mutant M-30 with enhanced inulinase production, mutant is stable after cultivation for 20 generations. Inulin, yeast extract, NaCl, temperature, pH for maximum inulinase production by the mutant M-30 are 20.0 g/l, 5.0 g/l, 20.0 g/l, at 28°C and pH 6.5, respectively. Under the optimized conditions, 127.7 U/ml of inulinase activity is reached in the liquid culture
synthesis
-
proposed kinetic model for fructose production defined within temperature and substrate concentration ranges of industrial interest such as 40-60°C and 3-60 g/l, respectively. Model is based on a minimum number of parameters. The hypotheses are always specified and assumed only on the basis of convenience and rational consideration. The kinetic model was successfully validated by comparison with a vast set of experimental results
synthesis
-
application of a bi-enzymatic system based on the combined use of levansucrase from Bacillus amyloliquefaciens and endo-inulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides and oligolevans using sucrose as the sole substrate. The optimal conditions leading to a high yield of short chain fructooligosaccharides, i.e.1:1 ratio, 0.5 h, 0.6 M, are different from those resulting in a high yield of medium chain fructooligosaccharides and oligolevans, i.e. 1.85:1 ratio, 1.77 h, 0.6 M. The production of fructooligosaccharides and oligolevans at a large scale gives a yield of 57-65%, w/w and produces 65.8-266.8 g/l and h, and uses of low temperature of 35°C and low concentrations of sucrose
synthesis
-
gene expression in Pichia pastoris using codon optimization results in the secretion of recombinant endoinulinase activity that reaches 1349 U/ml. Inulooligosaccharides production from inulin using the recombinant enzyme, after 8 h under optimal conditions, which include 400 g/l inulin, an enzyme concentration of 40 U/g substrate, 50°C and pH 6.0gives a yield of 91%
synthesis
-
growth of Aspergillus niger AUMC 9375 on the mixture of a 6:1 w/w ratio of sun flower tuber:lettuce roots, yields the highest levels of inulinase at 50% moisture, 30°C, pH 5.0, with seven days of incubation, and with yeast extract as the best nitrogen source. Purified inulinase is successfully immobilized with an immobilization yield of 71.28%. After incubation for 2 h at 60°C, the free enzyme activity decreases markedly to 10%, whereas that of the immobilized form decreases only to 87%. The immobilized inulinase can be used for 10 cycles and in addition, can be stored for 32 days at 4°C
synthesis
-
immobilization of endoinulinase results in higher stability than the free endoinulinase under various temperature levels. A residual activity of 81.2% can be still obtained after ten reaction cycles
synthesis
-
optimal grwoth conditions for expression of enzyme are 1% inulin,1% yeast extract, and 0.05% KH2PO4. Under optimum conditions, endoinulinase production reaches 28.67 IU/ml and biomass yield 0.162 OD600/15, in excellence correlation with predicted values. Endoinulinase production from a simple and cost-effective medium using raw Dahlia inulin is comparable with pure inulin
synthesis
-
endoinulinase is an inulolytic enzyme which is used for the production of fructooligosaccharides from inulin
synthesis
endoinulinases are an industrial tool critical for the production of inulooligosaccharides (IOS)
synthesis
enzymatic hydrolyzation of inulin by endo-inulinase to produce oligofructoses, a type of food additive and health product, a promising green and environmentally friendly technique
synthesis
enzymatic synthesis of fructooligosaccharides (FOS) from sucrose by endo-inulinase-catalyzed transfructosylation reaction in biphasic systems, production of FOS from sucrose by commercial inulinase from Aspergillus niger
synthesis
inulooligosaccharides (IOS) represent an important class of oligosaccharides at industrial scale. Efficient conversion of inulin to IOS through endoinulinase from Aspergillus niger
synthesis
-
enzymatic hydrolyzation of inulin by endo-inulinase to produce oligofructoses, a type of food additive and health product, a promising green and environmentally friendly technique
-
synthesis
-
inulooligosaccharides (IOS) represent an important class of oligosaccharides at industrial scale. Efficient conversion of inulin to IOS through endoinulinase from Aspergillus niger
-
synthesis
-
inulooligosaccharides (IOS) represent an important class of oligosaccharides at industrial scale. Efficient conversion of inulin to IOS through endoinulinase from Aspergillus niger
-
synthesis
-
optimal grwoth conditions for expression of enzyme are 1% inulin,1% yeast extract, and 0.05% KH2PO4. Under optimum conditions, endoinulinase production reaches 28.67 IU/ml and biomass yield 0.162 OD600/15, in excellence correlation with predicted values. Endoinulinase production from a simple and cost-effective medium using raw Dahlia inulin is comparable with pure inulin
-
synthesis
-
immobilization of endoinulinase results in higher stability than the free endoinulinase under various temperature levels. A residual activity of 81.2% can be still obtained after ten reaction cycles
-
synthesis
-
inulooligosaccharides (IOS) represent an important class of oligosaccharides at industrial scale. Efficient conversion of inulin to IOS through endoinulinase from Aspergillus niger
-
synthesis
-
endoinulinases are an industrial tool critical for the production of inulooligosaccharides (IOS)
-
synthesis
-
gene expression in Pichia pastoris using codon optimization results in the secretion of recombinant endoinulinase activity that reaches 1349 U/ml. Inulooligosaccharides production from inulin using the recombinant enzyme, after 8 h under optimal conditions, which include 400 g/l inulin, an enzyme concentration of 40 U/g substrate, 50°C and pH 6.0gives a yield of 91%
-
synthesis
-
growth of Aspergillus niger AUMC 9375 on the mixture of a 6:1 w/w ratio of sun flower tuber:lettuce roots, yields the highest levels of inulinase at 50% moisture, 30°C, pH 5.0, with seven days of incubation, and with yeast extract as the best nitrogen source. Purified inulinase is successfully immobilized with an immobilization yield of 71.28%. After incubation for 2 h at 60°C, the free enzyme activity decreases markedly to 10%, whereas that of the immobilized form decreases only to 87%. The immobilized inulinase can be used for 10 cycles and in addition, can be stored for 32 days at 4°C
-
synthesis
-
endoinulinase is an inulolytic enzyme which is used for the production of fructooligosaccharides from inulin
-
additional information
inulinase from Pichia guilliermondii strain 1 is closely related to that from Kluyveromyces marxianus
additional information
-
inulinase from Pichia guilliermondii strain 1 is closely related to that from Kluyveromyces marxianus
additional information
-
inulinase from Pichia guilliermondii strain 1 is closely related to that from Kluyveromyces marxianus
-
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Ettalibi, M.; Baratti, J.C.
Purification, properties and comparison of invertase, exoinulinase and endoinulinase of Aspergillus ficuum
Appl. Microbiol. Biotechnol.
26
13-20
1987
Aspergillus ficuum
-
brenda
Xiao, R.; Tanida, M.; Takao, S.
Purification and some properties of endoinulinase from Chrysosporium pannorum
J. Ferment. Bioeng.
67
244-248
1989
Pseudogymnoascus pannorum, Pseudogymnoascus pannorum AHU 9700
-
brenda
Nakamura, T.; Shitara, A.; Matsulda, S.; Matsuo, T.; Suiko, M.; Ohta, K.
Production, purification and properties of an endoinulinase of Penicillium sp. TN-88 that liberates inulotriose
J. Ferment. Bioeng.
84
313-318
1997
Penicillium sp., Penicillium sp. TN-88
-
brenda
Beck, R.H.F.; Praznik, W.
Determination of inulinase isoenzymes on polyacrylamide gels by activity staining
J. Chromatogr.
369
240-243
1986
Aspergillus sp.
-
brenda
Azhari, R.; Szlak, A.M.; Ilan, E.; Sideman, S.; Lotan, N.
Purification and characterization of endo- and exo-inulinase
Biotechnol. Appl. Biochem.
11
105-117
1989
Aspergillus sp.
-
brenda
Xiao, R.; Tanida, M.; Takao, S.
Inulinase from Chrysosporium pannorum
J. Ferment. Technol.
66
553-558
1988
Pseudogymnoascus pannorum, Pseudogymnoascus pannorum AHU 9700
-
brenda
Onodera, S.; Shiomi, N.
Purification and substrate specificity of endo-type inulinase from Penicillium purpurogenum
Agric. Biol. Chem.
52
2569-2576
1988
Talaromyces purpureogenus
-
brenda
Kang, S.I.; Chang, Y.J.; Oh, S.J.; Kim, S.I.
Purification and properties of an endo-inulinase from an Arthrobacter sp.
Biotechnol. Lett.
20
983-986
1998
Arthrobacter sp.
-
brenda
Ettalibi, M.; Baratti, J.C.
Molecular and kinetic properties of Aspergillus ficuum inulinases
Agric. Biol. Chem.
54
61-68
1990
Aspergillus ficuum
brenda
Jing, W.; Zhengyu, J.; Bo, J.; Xueming, X.
Separation and identification of exo- and endoinulinase from Aspergillus ficuum
Curr. Microbiol.
47
109-112
2003
Aspergillus ficuum, Aspergillus ficuum JNSP5-06
brenda
Zaita, N.; Fukushige, T.; Tokuda, M.; Ohta, K.; Nakamura, T.
Preparation and enzymatic properties of Aspergillus niger endoinulinase immobilized onto various polysaccharide supports
Food Sci. Technol. Res.
6
34-39
2000
Aspergillus niger, Aspergillus niger 12
brenda
Kushi, R.T.; Monti, R.; Contiero, J.
Production, purification and characterization of an extracellular inulinase from Kluyveromyces marxianus var. bulgaricus
J. Ind. Microbiol. Biotechnol.
25
63-69
2000
Kluyveromyces marxianus
-
brenda
Cho, Y.J.; Yun, J.W.
Purification and characterization of an endoinulinase from Xanthomonas oryzae No.5
Process Biochem.
37
1325-1331
2002
Xanthomonas oryzae, Xanthomonas oryzae No.5
-
brenda
Gill, P.K.; Manhas, R.K.; Singh, P.
Comparative analysis of thermostability of extracellular inulinase activity from Aspergillus fumigatus with commercially available (Novozyme) inulinase
Biores. Technol.
97
355-358
2006
Aspergillus fumigatus
brenda
Catana, R.; Ferreira, B.S.; Cabral, J.M.; Fernandes, P.
Immobilization of inulinase for sucrose hydrolysis
Food Chem.
91
517-520
2005
Aspergillus niger
brenda
Rocha, J.R.; Catana, R.; Ferreira, B.S.; Cabral, J.M.; Fernandes, P.
Design and characterization of an enzyme system for inulin hydrolysis
Food Chem.
95
77-82
2005
Aspergillus niger
-
brenda
El-Shouny, W.A.; El-Banna, T.E.; Mohamed, A.B.; El-Said, A.F.
Purification and characterization of an exoinulinase from Streptomyces griseus
New Egypt. J. Microbiol.
9
318-335
2004
Streptomyces griseus
-
brenda
Singh, R.S.; Bhermi, H.K.
Production of extracellular exoinulinase from Kluyveromyces marxianus YS-1 using root tubers of Asparagus officinalis
Biores. Technol.
99
7418-7423
2008
Kluyveromyces marxianus, Kluyveromyces marxianus Ys-1
brenda
Skowronek, M.; Fiedurek, J.
Purification and properties of extracellular endoinulinase from Aspergillus niger 20 OSM
Food Technol. Biotechnol.
44
53-58
2006
Aspergillus niger, Aspergillus niger 20 OSM
-
brenda
Moriyama, S.; Muguruma, M.; Ohta, K.
Quantitative expression analysis of inulinase gene cluster of Penicillium sp. strain TN-88
J. Biosci. Bioeng.
101
277-279
2006
Penicillium sp. (Q9HFA5), Penicillium sp., Penicillium sp. TN-88 (Q9HFA5)
brenda
Gao, L.; Chi, Z.; Sheng, J.; Wang, L.; Li, J.; Gong, F.
Inulinase-producing marine yeasts: evaluation of their diversity and inulin hydrolysis by their crude enzymes
Microb. Ecol.
54
722-729
2007
Yarrowia lipolytica, Yarrowia lipolytica OUC2
brenda
Zhang, T.; Gong, F.; Chi, Z.; Liu, G.; Chi, Z.; Sheng, J.; Li, J.; Wang, X.
Cloning and characterization of the inulinase gene from a marine yeast Pichia guilliermondii and its expression in Pichia pastoris
Antonie van Leeuwenhoek
95
13-22
2009
Meyerozyma guilliermondii (A5DHM6), Meyerozyma guilliermondii, Meyerozyma guilliermondii 1 (A5DHM6)
brenda
Tovar-Castro, L.; Garcia-Garibay, M.; Saucedo-Castaneda, G.
Lactase production by solid-state cultivation of Kluyveromyces marxianus CDBBL 278 on an inert support: effect of inoculum, buffer, and nitrogen source
Appl. Biochem. Biotechnol.
151
610-617
2008
Kluyveromyces marxianus, Kluyveromyces marxianus CDBBL 278
brenda
Gao, W.; Bao, Y.; Liu, Y.; Zhang, X.; Wang, J.; An, L.
Characterization of thermo-stable endoinulinase from a new strain Bacillus smithii T7
Appl. Biochem. Biotechnol.
157
498-506
2008
Bacillus smithii, Bacillus smithii T7
brenda
Chi, Z.; Chi, Z.; Zhang, T.; Liu, G.; Yue, L.
Inulinase-expressing microorganisms and applications of inulinases
Appl. Microbiol. Biotechnol.
82
211-220
2009
Penicillium sp., Pseudomonas sp., Pseudomonas mucidolens, Aspergillus niger (A5ABL2), Talaromyces purpureogenus (O00056), Aspergillus ficuum (O94220), Kluyveromyces marxianus (P28999), Arthrobacter sp. (Q9RBA5), Penicillium sp. TN-88, Aspergillus niger CBS 513.88 (A5ABL2)
brenda
Kim, K.Y.; Nascimento, A.S.; Golubev, A.M.; Polikarpov, I.; Kim, C.S.; Kang, S.I.; Kim, S.I.
Catalytic mechanism of inulinase from Arthrobacter sp. S37
Biochem. Biophys. Res. Commun.
371
600-605
2008
Arthrobacter sp. S37
brenda
Lima, D.M.; Oliveira, R.Q.; Uetanabaro, A.P.; Goes-Neto, A.; Rosa, C.A.; Assis, S.A.
Thermostable inulinases secreted by yeast and yeast-like strains from the Brazilian semi-arid region
Int. J. Food Sci. Nutr.
60
63-71
2009
Pseudozyma sp., Pseudozyma sp. CCMB 300
-
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Guo, N.; Gong, F.; Chi, Z.; Sheng, J.; Li, J.
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Aspergillus niger
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Aspergillus fumigatus, Aspergillus fumigatus Cl1
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Volkov, P.V.; Sinitsyna, O.A.; Fedorova, E.A.; Rojkova, A.M.; Satrutdinov, A.D.; Zorov, I.N.; Okunev, O.N.; Gusakov, A.V.; Sinitsyn, A.P.
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Aspergillus niger
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Aspergillus ficuum (O94220), Aspergillus ficuum
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Aspergillus ficuum (O94220), Aspergillus ficuum
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Aspergillus niger, Aspergillus niger CICIM F0620
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Talaromyces purpureogenus (O00056), Talaromyces purpureogenus, Talaromyces purpureogenus ATCC 4713 (O00056)
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Aspergillus arachidicola (A0A2G7G4Y0), Aspergillus arachidicola, Aspergillus arachidicola CBS 117610 (A0A2G7G4Y0)
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Aspergillus niger (A0A221C6S1), Aspergillus niger, Aspergillus niger CBS 120.49 (A0A221C6S1), Aspergillus niger DSM 2466 (A0A221C6S1), Aspergillus niger ATCC 9029 (A0A221C6S1)
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Genetic modification and optimization of endo-inulinase for the enzymatic production of oligofructose from inulin
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Fusarium oxysporum (A0A1B2CX88), Fusarium oxysporum ACCC31352 (A0A1B2CX88)
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PLoS ONE
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Aspergillus niger (O74641)
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