期刊
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
卷 86, 期 7, 页码 637-642出版社
WILEY
DOI: 10.1007/s11746-009-1401-8
关键词
Lipase; Cross-linked enzyme aggregates (CLEAs); Candida antarctica lipase B (CALB); Esterification activity; Immobilization
资金
- Department of Science & Technology (DST), India
- BOYSCAST fellowship
- Food-DTU
- Denmark Technical University
Commercially available microbial lipases from different sources were immobilized as cross-linked enzyme aggregates (CLEAs) using different precipitants and glutaraldehyde as cross-linkers. These CLEAs were assayed based on esterification between lauric acid and n-propanol in solvent-free systems. Precipitants were found to have a profound influence on both specific activities and total activity recovery of CLEAs, as exemplified by Candida antarctica lipase B (CALB). Among the CLEAs of CALB studied, those obtained using PEG600, ammonium sulfate, PEG200 and acetone as precipitants were observed to attain over 200% total activity recovery in comparison with acetone powder directly precipitated from the liquid solution by acetone. PEG200 precipitated CLEA gave the best specific activity (139% relative to acetone powder). The results of kinetic studies showed that V (max)/K (m) does not significantly change upon CLEA formation. This work presents a characterization of CLEAs based on an esterification activity assay, which is useful for exploring the synthetic application potential of CLEA technology with favorable perspectives.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据