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 (Comment) | Organism |
---|---|
gene lad1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Trichoderma reesei |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
soluble | - |
Trichoderma reesei | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Trichoderma reesei | Q96V44 | i.e Trichoderma reesei | - |
Trichoderma reesei YSM 768 | Q96V44 | i.e Trichoderma reesei | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Trichoderma reesei |
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 | Comment | Organism |
---|---|---|
More | three-dimensional structure homology modelling, overview | Trichoderma reesei |
Synonyms | Comment | Organism |
---|---|---|
HjLAD | - |
Trichoderma reesei |
L-arabinitol dehydrogenase | - |
Trichoderma reesei |
Lad1 | - |
Trichoderma reesei |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
both free and immobilized enzyme HjLAD | Trichoderma reesei |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 70 | activity range of both free and immobilized enzymes | Trichoderma reesei |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.5 | - |
assay at | Trichoderma reesei |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 10 | activity range of both free and immobilized enzymes | Trichoderma reesei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Trichoderma reesei |
General Information | Comment | Organism |
---|---|---|
additional information | three-dimensional structure homology modelling, overview | Trichoderma reesei |