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Immobilization of L-arabinitol Dehydrogenase on Aldehyde-Functionalized Silicon Oxide Nanoparticles for L-xylulose Production

Immobilization of L-arabinitol Dehydrogenase on Aldehyde-Functionalized Silicon Oxide Nanoparticles for L-xylulose Production

Raushan Kumar Singh, Manish Kumar Tiwari, Ranjitha Singh, Jung-Rim Haw, Jung-Kul Lee

Appl Microbiol Biotechnol. 2014 Feb;98(3):1095-104.

PMID: 24193245

Abstract:

L-Xylulose is a potential starting material for therapeutics. However, its translation into clinical practice has been hampered by its inherently low bioavailability. In addition, the high cost associated with the production of L-xylulose is a major factor hindering its rapid deployment beyond the laboratory. In the current study, L-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD), which catalyzes the conversion of L-arabinitol into L-xylulose, was immobilized onto various carriers, and the immobilized enzymes were characterized. HjLAD covalently immobilized onto silicon oxide nanoparticles showed the highest immobilization efficiency (94.7 %). This report presents a comparative characterization of free and immobilized HjLAD, including its thermostability and kinetic parameters. The thermostability of HjLAD immobilized on silicon oxide nanoparticles was more than 14.2-fold higher than free HjLAD; the t1/2 of HjLAD at 25 °C was enhanced from 190 min (free) to 45 h (immobilized). In addition, the immobilized HjLAD retained 94 % of its initial activity after 10 cycles. When the immobilized HjLAD was used to catalyze the biotransformation of L-arabinitol to L-xylulose, 66 % conversion and a productivity of 7.9 g · h(-1) · L(-1) were achieved. The enhanced thermostability and reusability of HjLAD suggest that immobilization of HjLAD onto silicon oxide nanoparticles has the potential for use in the industrial production of rare sugars.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP7643756-A	L-Arabinitol		7643-75-6	Price

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