Buffer-mediated activation of Candida antarctica lipase B dissolved in hydroxyl-functionalized ionic liquids

被引：21
|
作者：
Ou, Guangnan [1 ]
Yang, Jing [2 ,3 ]
He, Biyan [1 ]
Yuan, Youzhu [2 ,3 ]
机构：
[1] Jimei Univ, Sch Bioengn, Xiamen 361021, Peoples R China
[2] Xiamen Univ, Coll Chem & Chem Engn, State Key Lab Phys Chem Solid Surfaces, Xiamen 361005, Peoples R China
[3] Xiamen Univ, Coll Chem & Chem Engn, Natl Engn Lab Green Chem Prod Alcohols Ethers Est, Xiamen 361005, Peoples R China
来源：
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2011年 / 68卷 / 01期
关键词：
Ionic-liquid buffer; Hydroxyl-functionalized ionic liquid; Lipase; Fluorescence; ENZYME CATALYSIS; ORGANIC-SOLVENTS; PROTEIN CORE; STABILITY; BIOCATALYSIS; ACID; CONSEQUENCES; REPLACEMENTS; LYSOZYME; CHARGE;
D O I：
10.1016/j.molcatb.2010.09.013
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：
Ionic-liquid buffer having phosphate anion was synthesized for the development of buffered enzymatic ionic liquid systems Both the conformation and transesterification activity of Candida antarctica lipase B (CALB) dissolved in the hydroxyl-functionalized ionic liquids were buffer dependent Intrinsic fluorescence studies indicated that the CALB possessed a more compact conformation in the medium consisted of ionic liquid buffer having phosphate anion and hydroxyl-functionalized ionic liquids like 1-(1-hydroxyethyl)-3-methyl-imidazolium tetrafluoroborate and 1-(1-hydroxyethyl)-3-methyl-imidazolium nitrate High activity and outstanding stability could be obtained with the CALB enzyme in the buffered ionic liquids for the transesterification (c) 2010 Elsevier B V All rights reserved
引用
收藏
页码：66 / 70
页数：5
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