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Immobilization of lipase by salts and the transesterification activity in hexane

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Abstract

Lipases from six different sources were immobilized on Celite and five types of salt. The transesterification activities in hexane for lipases immobilized on EDTA-Na2 increased by 463% for the lipase from Candida rugosa (CRL), 2700% for the lipase from Candida sp. (CSL) and 1215% for the lipase from Pseudomonas sp. (PSL), compared to the salt-free enzyme. With 0.5% sucrose for CRL or 1% sorbitol for PSL as the lyoprotectant during lyophilization process, transesterification activity increased by 100% and 13%, respectively, compared to the immobilized enzyme on EDTA-Na2 without lyoprotectant.

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Authors and Affiliations

  1. School of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, 310014, P.R. China

    Wang Pu

  2. Institute of Biochemical Engineering, College of Material Science & Chemical Engineering, Yuquan Campus, Zhejiang University, Hangzhou, 310027, P.R. China

    Yang Li-rong & Wu Jian-ping

Authors
  1. Wang Pu
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  2. Yang Li-rong
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  3. Wu Jian-ping
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Pu, W., Li-rong, Y. & Jian-ping, W. Immobilization of lipase by salts and the transesterification activity in hexane. Biotechnology Letters 23, 1429–1433 (2001). https://doi.org/10.1023/A:1011630216527

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  • DOI: https://doi.org/10.1023/A:1011630216527

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