Immobilization of lipase on aminopropyl-grafted mesoporous silica nanotubes for the resolution of (R, S)-1-phenylethanol

被引：31

作者：

Bai, Wei ^{[2
,3
]}

Yang, Yun-Jie ^{[1
]}

Tao, Xia ^{[1
]}

Chen, Jian-Feng ^{[1
]}

Tan, Tian-Wei ^{[2
]}

机构：

[1] Beijing Univ Chem Technol, Minist Educ, Key Lab Nanomat, Beijing 100029, Peoples R China

[2] Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R China

[3] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2012年 / 76卷

关键词：

Lipase; Immobilization; Mesoporous silica nanotubes; Aminopropyl-grafted; Phenylethanol; ENZYME IMMOBILIZATION; CATALYTIC-PROPERTIES; NANOPOROUS SUPPORT; SBA-15; ADSORPTION; SURFACES;

D O I：

10.1016/j.molcatb.2011.11.005

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：

Mesoporous silica nanotubes and aminopropyl-grafted mesoporous silica nanotubes were prepared as supports to immobilize lipase from Candida sp. 99-125(CILip) by physical adsorption. The immobilization conditions were investigated. Moreover, immobilized lipases on both kinds of supports were employed to catalyze olive oil hydrolization and resolution of 1-phenylethanol by esterification. The results showed that the hydrolization activity of the lipase immobilized on aminopropyl-grafted mesoporous silica nanotubes was almost twice of that on mesoporous silica nanotubes. In addition, the resolution of 1-phenylethanol catalyzed by the former catalyst also increased 22%. Circular dichroism spectra revealed a reduction of alpha-helix and an increase of beta-sheet when lipase was adsorbed on aminopropyl-grafted mesoporous silica nanotubes, which suggested that parts of alpha-helix were extended and reformed to be beta-sheet. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：82 / 88

页数：7

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