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2-chloro-4-nitrophenyl maltotriosyl-alpha(1->6)-maltotriosyl-beta-D-glucose + H2O
2-chloro-4-nitrophenyl maltotriose + maltotriosyl-beta-D-glucose
-
-
-
-
?
4,6-O-benzylidene-2-chloro-4-nitrophenyl-beta-63-alpha-D-maltotriosyl-maltotrioside + H2O
4,6-O-benzylidene-D-maltotriose + 4-nitrophenyl beta-D-maltotriose
-
substrate is not susceptible to transglycosylation and may serve as a routine quantitative assay tool
-
-
?
4,6-O-benzylidene-4-methylumbelliferyl-beta-63-alpha-D-maltotriosyl-maltotrioside
4,6-O-benzylidene-D-maltotriose + 4-methylumbelliferyl beta-D-maltotriose
-
substrate is susceptible to transglycosylation and may serve as a routine quantitative assay tool
-
-
?
6-alpha-maltosylmaltotetraose + H2O
?
-
-
-
-
?
6-alpha-maltosylmaltotriose + H2O
?
-
-
-
-
?
6-alpha-maltotriosylmaltotetraose + H2O
?
amylase + H2O
?
-
-
-
-
?
amylopectin + H2O
maltotriose + maltose + maltooligosaccharides
6.0% of the activity with pullulan
-
-
?
amylopectin beta-limit dextrin + H2O
maltotriose + maltose + maltooligosaccharides
beta-limited dextrin + H2O
maltotriose + maltose + maltooligosaccharides
19.7% of the activity with pullulan
-
-
?
dextrin + H2O
?
-
-
-
-
?
glycogen + H2O
maltotriose + maltose + maltooligosaccharides
6.1% of the activity with pullulan
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltooligosaccharides
-
-
-
-
?
limit dextrin + H2O
maltotriose + maltotetraose + maltopentaose
limit dextrins + H2O
?
-
limit dextrinase catalyzes the hydrolysis of alpha-1,6 glucosidic linkages in limit dextrins
-
-
?
polysaccharide + H2O
oligosaccharides
pullulan + H2O
maltotriose + ?
soluble starch + H2O
maltotriose + maltose + maltooligosaccharides
12.8% of the activity with pullulan
-
-
?
additional information
?
-
6-alpha-maltotriosylmaltotetraose + H2O
?
-
-
-
-
?
6-alpha-maltotriosylmaltotetraose + H2O
?
-
-
-
-
?
6-alpha-maltotriosylmaltotetraose + H2O
?
-
-
-
-
?
6-alpha-maltotriosylmaltotetraose + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin beta-limit dextrin + H2O
maltotriose + maltose + maltooligosaccharides
-
-
-
-
?
amylopectin beta-limit dextrin + H2O
maltotriose + maltose + maltooligosaccharides
-
-
-
-
?
amylopectin beta-limit dextrin + H2O
maltotriose + maltose + maltooligosaccharides
-
-
-
-
?
limit dextrin + H2O
?
-
-
-
-
?
limit dextrin + H2O
?
the enzyme hydrolyses alpha-1,6-glucosidic linkages in limit dextrins derived from amylopectin
-
-
?
limit dextrin + H2O
maltotriose + maltotetraose + maltopentaose
EPZ37738
-
-
-
?
limit dextrin + H2O
maltotriose + maltotetraose + maltopentaose
EPZ37738
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
natural substrates appear to be alpha-limit dextrins
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
-
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
polysaccharide + H2O
oligosaccharides
-
oligosaccharides containing maltosyl or larger side chains are hydrolysed as well as amylopectin and amylopectin beta-limit dextrin, oligo- and poly-saccharides containing single D-glucosyl groups attached by an alpha-(1,6) linkage to the rest of the molecule are not hydrolysed, glycogen is not a substrate
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
-
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
-
-
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
additional information
?
-
EPZ37738
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. Main reaction is as a type I pullulanase, EC 3.2.1.41
-
-
?
additional information
?
-
EPZ37738
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. Main reaction is as a type I pullulanase, EC 3.2.1.41
-
-
?
additional information
?
-
no substrates: maltotriose, maltose. the enzyme is strictly restricted to hydrolysis of 1->6-linked glucosidic linkages. It also acts as type I pullulanase, EC 3.2.1.41
-
-
?
additional information
?
-
-
the enzyme has low activity towards amylopectin
-
-
?
additional information
?
-
-
no activity with glycogen
-
-
?
additional information
?
-
-
release of glucose reducing-sugar equivalents from pullulan
-
-
?
additional information
?
-
-
the debranching enzyme limit dextrinase, also known as pullulanase, catalyses hydrolysis of alpha-1,6-glucosidic bonds
-
-
?
additional information
?
-
-
the enzyme displays transglycosylation activity
-
-
?
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2-mercaptoethanol
5 mM, 51% residual activity
6,3-alpha-D-glucosylmaltotriose
-
-
6,3-alpha-D-maltosylmaltotetraose
-
-
6,3-alpha-D-maltosylmaltotriose
-
-
6,3-alpha-D-maltotriosylmaltotetraose
-
-
6,3-alpha-D-maltotriosylmaltotriose
-
-
Ba2+
EPZ37738
2 mM, 54% of initial activtiy
Co2+
EPZ37738
2 mM, 15% of initial activtiy
cyclohexaamylose
-
competitive inhibition
Mg2+
5 mM, 90% residual activity
Mn2+
EPZ37738
2 mM, 40% of initial activtiy
NH4+
EPZ37738
2 mM, 49% of initial activtiy
Ni2+
EPZ37738
2 mM, 47% of initial activtiy
SDS
5 mM, 46% residual activity
Sr2+
EPZ37738
2 mM, 73% of initial activtiy
Triton X-100
EPZ37738
1% v/v, 72% of initial activtiy
Urea
EPZ37738
2 mM, 57% of initial activtiy
additional information
-
a specific inhibitor of limit dextrinase is found in mature barley kernels, but disappears after several days of germination. Two forms of this proteinaceous inhibitor, identical in amino acid sequence, are isolated and characterized. They differ in attachment of cysteine or glutathione to a sulfhydryl group, possibly that of cysteine residue 59 of the inhibitor. They can form a 1:1 complex with limit dextrinase and are believed to interact specifically with the active site of the enzyme
-
alpha-cyclodextrin
-
competitive inhibitor
alpha-cyclodextrin
competitive inhibitor
beta-cyclodextrin
-
competitive inhibitor
beta-cyclodextrin
competitive inhibitor
Cu2+
EPZ37738
2 mM, 8% of initial activtiy
Cu2+
5 mM, 67% residual activity
EDTA
EPZ37738
2 mM, 68% of initial activtiy
EDTA
5 mM, 72% residual activity
Fe2+
EPZ37738
2 mM, 6% of initial activtiy
Zn2+
EPZ37738
2 mM, 22% of initial activtiy
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0.135 - 0.154
2-chloro-4-nitrophenyl maltotriosyl-alpha(1->6)-maltotriosyl-beta-D-glucose
0.192
4,6-O-benzylidene-2-chloro-4-nitrophenyl-beta-63-alpha-D-maltotriosyl-maltotrioside
-
pH.0, 40°C
0.052
4,6-O-benzylidene-4-methylumbelliferyl-beta-63-alpha-D-maltotriosyl-maltotrioside
-
pH.0, 40°C
0.2
6-alpha-maltosylmaltotetraose
-
-
0.2
6-alpha-maltosylmaltotriose
-
-
0.16 - 1.5
6-alpha-maltotriosylmaltotetraose
0.2
6-alpha-maltotriosylmaltotriose
-
-
0.6 - 3.24
amylopectin beta-limit dextrin
-
26
glycogen beta-limit dextrin
-
-
-
additional information
amylopectin
0.135
2-chloro-4-nitrophenyl maltotriosyl-alpha(1->6)-maltotriosyl-beta-D-glucose
-
pH 5.3, 45°C, barley malt extract
0.154
2-chloro-4-nitrophenyl maltotriosyl-alpha(1->6)-maltotriosyl-beta-D-glucose
-
pH 5.3, 45°C, recombinant enzyme
0.16
6-alpha-maltotriosylmaltotetraose
-
-
0.2
6-alpha-maltotriosylmaltotetraose
-
-
0.6
6-alpha-maltotriosylmaltotetraose
-
-
1.5
6-alpha-maltotriosylmaltotetraose
-
-
0.6
amylopectin beta-limit dextrin
-
-
-
1.5
amylopectin beta-limit dextrin
-
-
-
3.24
amylopectin beta-limit dextrin
-
-
-
additional information
amylopectin
Km value of wild-type 6.9 mg/ml, mutant M440G 4.4 mg/ml, respectively, 37°C, pH not specified in the publication
additional information
amylopectin
-
Km value of wild-type 6.9 mg/ml, mutant M440G 4.4 mg/ml, respectively, 37°C, pH not specified in the publication
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
classical Michaelis-Menten kinetics results in Km of 0.081 mg/ml, fitting the uncompetitive substrate inhibition Michaelis-Menten equation results in Km 0.16 mg/ml, pH 5.5, 40°C
-
additional information
additional information
-
classical Michaelis-Menten kinetics results in Km of 0.081 mg/ml, fitting the uncompetitive substrate inhibition Michaelis-Menten equation results in Km 0.16 mg/ml, pH 5.5, 40°C
-
additional information
pullulan
Km value 0.12 mg/ml, pH 6.0, 50°C
additional information
pullulan
Km value of wild-type 0.16 mg/ml, mutant M440G 0.15 mg/ml, respectively, 37°C, pH not specified in the publication
additional information
pullulan
-
Km value of wild-type 0.16 mg/ml, mutant M440G 0.15 mg/ml, respectively, 37°C, pH not specified in the publication
additional information
soluble starch
Km value 0.69 mg/ml,pH 6.0, 50°C
-
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A885S
single nucleotide polymorphism associated with thermostability
D730R
modest change in the association rate constant with endogenous inhibitor LDI. Residue D730 binds in a positively charged pocket on the surface of LDI via a hydrogen bond and a salt bridge to residue Arg34 and a hydrogen bond to Arg84 of LDI. D730 adopts different rotamers in the free enzyme and enzyme bound to LDI
D730W
modest change in the association rate constant with endogenous inhibitor LDI. Residue D730 binds in a positively charged pocket on the surface of LDI via a hydrogen bond and a salt bridge to residue Arg34 and a hydrogen bond to Arg84 of LDI. D730 adopts different rotamers in the free enzyme and enzyme bound to LDI
E510A
0.0004% residual activity with pullulan
L102R/T233A/S235G/G298A/C415R/A885S/G888C
amino acid substitutions identified by alignment of the limit dextrinase sequences of varieties Galleon and Maud
M440G
2.6fold decrease in catalytic efficiency
T233A
single nucleotide polymorphism associated with thermostability
additional information
EPZ37738
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
additional information
-
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
-
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity
additional information
investigation on genetic diversity of limit dextrinase using single strand conformation polymorphism based on the amino acid substitutions. Only limited genetic variation is detected in the current malting barley varieties, although wide variation is observed in the wider barley germplasm. No polymorphism is associated with the enzyme activity
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Kristensen, M.; Lok, F.; Planchot, V.; Svendsen, I.; Leah, R.; Svensson, B.
Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley
Biochim. Biophys. Acta
1431
538-546
1999
Hordeum vulgare
brenda
Manners, D.J.
Observation on the specificity and nomenclature of starch debranching enzymes
J. Appl. Glycosci.
44
83-85
1997
Avena sativa, Vicia faba, Hordeum vulgare, Oryza sativa, Pisum sativum, Sorghum bicolor
-
brenda
Yellowlees, D.
Purification and characterization of limit dextrinase from Pisum sativum L.
Carbohydr. Res.
83
109-118
1980
Pisum sativum
brenda
Hardie, D.G.; Manners, D.J.; Yellowlees, D.
The limit dextrinase from malted sorghum (Sorghum vulgare)
Carbohydr. Res.
50
75-85
1976
Sorghum bicolor
brenda
Dunn, G.; Manners, D.J.
The limit dextrinase from ungerminated oats (Avena sativa L.) and ungerminated rice (Oryza sativa L.)
Carbohydr. Res.
39
283-293
1975
Avena sativa, Oryza sativa
brenda
Gordon, R.W.; Manners, D.J.; Stark, J.R.
The limit dextrinase of the broad bean (Vicia faba L.)
Carbohydr. Res.
42
125-134
1975
Vicia faba
-
brenda
MacGregor, E.A.
The proteinaceous inhibitor of limit dextrinase in barley and malt
Biochim. Biophys. Acta
1696
165-170
2004
Hordeum vulgare
brenda
Evans, D.; Dambergs, R.; Ratkowsky, D.; Li, C.; Harasymow, S.; Roumeliotis, S.; Eglinton, J.
Refining the prediction of potential malt fermentability by including an assessment of limit dextrinase thermostability and additional measures of malt modification, using two different methods for multivariate model development
J. Inst. Brew.
116
86-96
2010
Hordeum vulgare (O48541)
-
brenda
Yang, X.; Westcott, S.; Gong, X.; Evans, E.; Zhang, X.; Lance, R.; Li, C.
Amino acid substitutions of the limit dextrinase gene in barley are associated with enzyme thermostability
Mol. Breed.
23
61-74
2009
Hordeum vulgare (O48541), Hordeum vulgare (Q9FYY0), Hordeum vulgare (Q9S7S8)
-
brenda
Vester-Christensen, M.B.; Hachem, M.A.; Naested, H.; Svensson, B.
Secretory expression of functional barley limit dextrinase by Pichia pastoris using high cell-density fermentation
Protein Expr. Purif.
69
112-119
2010
Hordeum vulgare (O48541), Hordeum vulgare
brenda
Vester-Christensen, M.B.; Abou Hachem, M.; Svensson, B.; Henriksen, A.
Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins
J. Mol. Biol.
403
739-750
2010
Hordeum vulgare
brenda
Moeller, M.S.; Abou Hachem, M.; Svensson, B.; Henriksen, A.
Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
Acta Crystallogr. Sect. F
68
1008-1012
2012
Hordeum vulgare (O48541), Hordeum vulgare
brenda
Peng, Y.; Hu, F.
Purification and characterization of limit dextrinase from malted barley
AIDS Res. Hum. Retroviruses
550-553
1747-1754
2012
Hordeum vulgare
-
brenda
Boejstrup, M.; Christensen, C.E.; Windahl, M.S.; Henriksen, A.; Hindsgaul, O.
A chromogenic assay for limit dextrinase and pullulanase activity
Anal. Biochem.
449
45-51
2014
Hordeum vulgare
brenda
Jin, X.; Cai, S.; Ye, L.; Chen, Z.; Zhou, M.; Zhang, G.
Association of HvLDI with limit dextrinase activity and malt quality in barley
Biotechnol. Lett.
35
639-645
2013
Hordeum vulgare
brenda
Gebremariam, M.; Zarnkow, M.; Becker, T.
Effect of drying temperature and time on alpha-amylase, beta-amylase, limit dextrinase activities and dimethyl sulphide level of teff (Eragrostis tef) malt
Food Bioproc. Technol.
6
3462-3472
2013
Eragrostis tef
-
brenda
Henson, C.; Duke, S.; Vinje, M.
A comparison of barley malt amylolytic enzyme thermostabilities and wort sugars produced during mashing
J. Am. Soc. Brew. Chem.
72
51-65
2014
Hordeum vulgare
-
brenda
Shahpiri, A.; Talaei, N.; Finnie, C.
Spatio-temporal appearance of alpha-amylase and limit dextrinase in barley aleurone layer in response to gibberellic acid, abscisic acid and salicylic acid
J. Sci. Food Agric.
95
141-147
2015
Hordeum vulgare
brenda
Kahar, U.M.; Ng, C.L.; Chan, K.G.; Goh, K.M.
Characterization of a type I pullulanase from Anoxybacillus sp. SK3-4 reveals an unusual substrate hydrolysis
Appl. Microbiol. Biotechnol.
100
6291-6307
2016
Anoxybacillus sp. (EPZ37738), Anoxybacillus sp. SK3-4 (EPZ37738)
brenda
Bojstrup, M.; Marri, L.; Lok, F.; Hindsgaul, O.
A chromogenic assay suitable for high-throughput determination of limit dextrinase activity in barley malt extracts
J. Agric. Food Chem.
63
10873-10878
2015
Hordeum vulgare
brenda
Moller, M.S.; Vester-Christensen, M.B.; Jensen, J.M.; Hachem, M.A.; Henriksen, A.; Svensson, B.
Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal type inhibitors
J. Biol. Chem.
290
12614-12629
2015
Hordeum vulgare (O48541), Hordeum vulgare
brenda
Mangan, D.; McCleary, B.; Cornaggia, C.; Ivory, R.; Rooney, E.; McKie, V.
Colourimetric and fluorimetric substrates for the assay of limit dextrinase
J. Cereal Sci.
62
50-57
2015
Oryza sativa
-
brenda
Moller, M.S.; Windahl, M.S.; Sim, L.; Bojstrup, M.; Abou Hachem, M.; Hindsgaul, O.; Palcic, M.; Svensson, B.; Henriksen, A.
Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase
J. Mol. Biol.
427
1263-1277
2015
Hordeum vulgare (O48541), Hordeum vulgare
brenda
Qiao, Y.; Peng, Q.; Yan, J.; Wang, H.; Ding, H.; Shi, B.
Gene cloning and enzymatic characterization of alkali-tolerant type I pullulanase from Exiguobacterium acetylicum
Lett. Appl. Microbiol.
60
52-59
2015
Exiguobacterium acetylicum (I3WU34), Exiguobacterium acetylicum YH5 (I3WU34)
brenda
Siapush, S.; Shahpiri, A.
Ethephon advances the release time of limit dextrinase from gibberellic acid-treated aleurone layer
Biocatal. Agricult. Biotechnol.
9
174-176
2017
Hordeum vulgare
-
brenda
Moller, M.S.; Henriksen, A.; Svensson, B.
Structure and function of alpha-glucan debranching enzymes
Cell. Mol. Life Sci.
73
2619-2641
2016
Klebsiella pneumoniae
brenda
Nguemogne, A.; Desobgo, Z.; Nso, E.
Comparative study of limit dextrinase potential of three sorghum cultivars (Safrari, Madjeru, and S.35)
J. Am. Soc. Brew. Chem.
75
255-261
2017
Sorghum bicolor
-
brenda
Huang, Y.; Cai, S.; Zhang, G.
The relationship of limit dextrinase, limit dextrinase inhibitor and malt quality parameters in barley and their genetic analysis
J. Cereal Sci.
70
140-145
2016
Hordeum vulgare
-
brenda
Gous, P.; Fox, G.
Review Amylopectin synthesis and hydrolysis Understanding isoamylase and limit dextrinase and their impact on starch structure on barley (Hordeum vulgare) quality
Trends Food Sci. Technol.
62
23-32
2017
Hordeum vulgare
-
brenda