Pretreatment of immobilized Candida sp 99-125 lipase to improve its methanol tolerance for biodiesel production

被引：45

作者：

Lu, Jike ^{[1
]}

Deng, Li ^{[1
]}

Zhao, Rui ^{[1
]}

Zhang, Ruisi ^{[1
]}

Wang, Fang ^{[1
]}

Tan, Tianwei ^{[1
]}

机构：

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

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2010年 / 62卷 / 01期

基金：

国家高技术研究发展计划(863计划);

关键词：

Pretreatment; Immobilized lipase; Biodiesel; Methanol tolerance; ORGANIC-SOLVENT SYSTEM; RUGOSA LIPASE; ENZYMATIC ALCOHOLYSIS; GLYCEROL TRIOLEATE; WATER; OIL; TRANSESTERIFICATION; ENANTIOSELECTIVITY; SP-99-125; ESTERS;

D O I：

10.1016/j.molcatb.2009.08.002

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：

Candida sp. 99-125 lipase immobilized on textile membrane was pretreated with several methods to improve its activity and methanol tolerance for biodiesel production. Lipase pretreatments with short chain alcohols from n-propyl alcohol to isobutyl alcohol did not have any positive effect on the lipase activity and methanol tolerance. While lipase treated with methanol solutions from 10 to 20% volume concentrations did enhance the enzyme activity and methanol tolerance, and this lipase activation effect did not exist when methanol volume concentration was 40%. 1 mM salt solutions of (NH4)(2)SO4, CaCl2, KCl, K2SO4 and MgCl2 pretreatments were the useful tools to improve the lipase activity and methanol tolerance. The reason might be that salts could incorporate with the protein molecular to form a more stable molecular to resist conformation change induced by high methanol concentration. The operational stability of pretreated lipase was improved dramatically for biodiesel production during batch reactions. (C) 2009 Published by Elsevier B.V.

引用

页码：15 / 18

页数：4

共 18 条

[1] Regeneration of immobilized Candida antarctica lipase for transesterification [J].