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Literature summary for 1.1.1.12 extracted from

  • Singh, R.K.; Tiwari, M.K.; Singh, R.; Haw, J.R.; Lee, J.K.
    Immobilization of L-arabinitol dehydrogenase on aldehyde-functionalized silicon oxide nanoparticles for L-xylulose production (2014), Appl. Microbiol. Biotechnol., 98, 1095-1104.
    View publication on PubMed

Application

Application Comment Organism
additional information covalent immobilization of purified enzyme HjLAD onto glutaraldehyde-activated silicon oxide nanoparticles shows the a high immobilization efficiency of 94.7%, comparative characterization of free and immobilized enzyme HjLAD, including its thermostability and kinetic parameters, overview. Thermostability of immobilized enzyme is 14.2-fold higher than for free HjLAD, the t1/2 of HjLAD at 25°C is enhanced from 190 min (free) to 45 h (immobilized). The immobilized HjLAD retains 94% of its initial activity after 10 cycles. Immobilization efficiencies of HjLAD onto different supports, silicon oxide nanoparticles (4830HT) show the highest efficiency, method optimization, overview Trichoderma reesei
synthesis immobilization of HjLAD onto silicon oxide nanoparticles has the potential for use in the industrial production of rare sugars, e.g. L-xylulose, due to the thermostability and reusability of the immobilized enzyme Trichoderma reesei

Cloned(Commentary)

Cloned (Comment) Organism
gene lad1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Trichoderma reesei

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Trichoderma reesei
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arabinitol + NAD+ Trichoderma reesei
-
L-xylulose + NADH + H+
-
?
L-arabinitol + NAD+ Trichoderma reesei YSM 768
-
L-xylulose + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Trichoderma reesei Q96V44 i.e Trichoderma reesei
-
Trichoderma reesei YSM 768 Q96V44 i.e Trichoderma reesei
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arabinitol + NAD+
-
Trichoderma reesei L-xylulose + NADH + H+
-
?
L-arabinitol + NAD+
-
Trichoderma reesei YSM 768 L-xylulose + NADH + H+
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure homology modelling, overview Trichoderma reesei

Synonyms

Synonyms Comment Organism
HjLAD
-
Trichoderma reesei
L-arabinitol dehydrogenase
-
Trichoderma reesei
Lad1
-
Trichoderma reesei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
both free and immobilized enzyme HjLAD Trichoderma reesei

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 70 activity range of both free and immobilized enzymes Trichoderma reesei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
half-life of free enzyme is 190 min, of immobilized enzyme 31.5 h Trichoderma reesei
30
-
half-life of free enzyme is 165 min, of immobilized enzyme 24.5 h Trichoderma reesei
40
-
half-life of free enzyme is 26 min, of immobilized enzyme 4.25 h Trichoderma reesei
50
-
half-life of free enzyme is 20 min, of immobilized enzyme 3.17 h Trichoderma reesei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
assay at Trichoderma reesei

pH Range

pH Minimum pH Maximum Comment Organism
6 10 activity range of both free and immobilized enzymes Trichoderma reesei

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Trichoderma reesei

General Information

General Information Comment Organism
additional information three-dimensional structure homology modelling, overview Trichoderma reesei