Active biocatalysts based on Candida rugosa lipase immobilized in vesicular silica

被引：59

作者：

Wu, Cuicui ^{[1
]}

Zhou, Guowei ^{[1
]}

Jiang, Xiaojie ^{[1
]}

Ma, Jingyun ^{[1
]}

Zhang, Huayong ^{[1
]}

Song, Hongbin ^{[1
]}

机构：

[1] Shandong Polytech Univ, Sch Chem, Shandong Univ, Key Lab Fine Chem, Jinan 250353, Peoples R China

来源：

PROCESS BIOCHEMISTRY | 2012年 / 47卷 / 06期

基金：

中国国家自然科学基金;

关键词：

Vesicular silica; Candida rugosa lipase; Immobilization; Activity; Thermal stability; MESOPOROUS SILICA; NANOPARTICLES; FABRICATION; CATALYSIS; PROTEINS; SUPPORTS; ENZYME; SBA-15;

D O I：

10.1016/j.procbio.2012.03.004

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：

Vesicular silica (VS) with hierarchical structure was prepared by utilizing cationic surfactant cetyltrimethylammonium bromide (CTAB) and anionic surfactant sodium dodecyl sulfate (SDS) as the structure directing agents, and 1,3,5-triisopropylbenzene (TIPB) as the micelle expander. The resulting unilamellar and multilamellar VS with interlamellar mean mesopore size of 15-20nm and shell thickness of 5-15 nm were used as supports for immobilization of Candida rugosa lipase (CRL) through physical adsorption. Possible mechanisms for the formation of VS and the immobilization of CRL on VS are proposed. N-2 adsorption-desorption experiments and Fourier transform infrared spectroscopy (FT-IR) measurements demonstrated that CRL was adsorbed into the curved channels of the VS. The catalytic activity, thermal stability, and reusability of VS immobilized CRL were assayed in phosphate buffer medium by hydrolysis of triacetin. The effects of pH and temperature on enzyme activity were also investigated. We report that VS immobilized CRL exhibited outstanding adaptability at higher pH and temperature, and excellent thermal stability and reusability compared with free CRL. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：953 / 959

页数：7

共 40 条

[1] Covalent immobilization of triacylglycerol lipase onto functionalized nanoscale SiO2 spheres [J].