Immobilized Lipase from Candida sp 99-125 on Hydrophobic Silicate: Characterization and Applications

被引：7

作者：

Zhao, Bin ^{[1
]}

Liu, Xinlong ^{[1
]}

Jiang, Yanjun ^{[1
]}

Zhou, Liya ^{[1
]}

He, Ying ^{[1
]}

Gao, Jing ^{[1
]}

机构：

[1] Hebei Univ Technol, Sch Chem Engn & Technol, Tianjin 300130, Peoples R China

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2014年 / 173卷 / 07期

关键词：

Lipase; Hydrophobic silicates; Immobilized enzymes; Stability; Biodiesel; MESOPOROUS SILICA; ENZYME IMMOBILIZATION; BIODIESEL PRODUCTION; COVALENT ATTACHMENT; CATALYTIC ACTIVITY; STABILITY; ORGANOSILICAS; ADSORPTION; SUPPORTS; BIOCATALYSIS;

D O I：

10.1007/s12010-014-0967-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Lipase Candida sp. 99-125 has been proved to be quite effective in catalyzing organic synthesis reactions and is much cheaper than commercial lipases. Mesoporous silicates are attractive materials for the immobilization of enzymes due to their unique structures. The present research designed a hydrophobic silicate with uniform pore size suitable for the comfort of lipase Candida sp. 99-125 for improving its activity and stability. The resulting immobilized lipase (LP@PMO) by adsorption was employed to catalyze hydrolysis, esterification, and transesterification reactions, and the performances were compared with the lipase immobilized on hydrophilic silicate (LP@PMS) and native lipase. The LP@PMO showed as high activity as that of native lipase in hydrolysis and much increased catalytic activity and reusability in the reactions for biodiesel production. Besides, LP@PMO also possessed better organic stability. Such results demonstrate that immobilization of lipase onto hydrophobic supports is a promising strategy to fabricate highly active and stable biocatalysts for applications.

引用

页码：1802 / 1814

页数：13

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