Characterization of Cross‐Linked Lipase Aggregates
Abstract 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 s...
| Published in: | Journal of the American Oil Chemists' Society |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2009
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1007/s11746-009-1401-8 https://onlinelibrary.wiley.com/doi/full/10.1007/s11746-009-1401-8 |
| Summary: | Abstract 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. |
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