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
收藏
页码：82 / 88
页数：7
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