1.1.1.12: L-arabinitol 4-dehydrogenase
This is an abbreviated version!
For detailed information about L-arabinitol 4-dehydrogenase, go to the full flat file.
Reaction
Synonyms
ADH, dehydrogenase, L-arabinitol, HjLAD, L-arabinitol dehydrogenase, L-arabitol dehydrogenase, LAD, Lad1, LADA, More, NAD(P)+-dependent arabitol dehydrogenase, pentitol-DPN dehydrogenase, XYL2
ECTree
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Application
Application on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase
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analysis
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enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate
synthesis
additional information
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
synthesis
rare L-sugar L-xylulose is produced by the enzymatic oxidation of arabinitol to give a yield of approximately 86%
synthesis
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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
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synthesis
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rare L-sugar L-xylulose is produced by the enzymatic oxidation of arabinitol to give a yield of approximately 86%
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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
additional information
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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
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
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