Characterization of Cross-Linked Lipase Aggregates

Autor: B. L. A. Prabhavathi Devi, Zheng Guo, Xuebing Xu
Rok vydání: 2009
Předmět:
Zdroj: Journal of the American Oil Chemists' Society. 86:637-642
ISSN: 1558-9331
0003-021X
DOI: 10.1007/s11746-009-1401-8
Popis: 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.
Databáze: OpenAIRE
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