Immobilization of cross-linked laccase by sodium alginate-gelatin for degradation bisphenol A in bubbling reactor

  • WEI Shenghua ,
  • SHEN Qi ,
  • QIN Mengru ,
  • ZHANG Huiyun ,
  • TANG Zhongxun ,
  • LI Song ,
  • MENG Na
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  • (School of Biological and Food Engineering, Anhui Polytechnic University, Wuhu 241000, China)

Received date: 2022-03-23

  Revised date: 2022-05-03

  Online published: 2023-02-14

Abstract

In order to improve the stability of laccase, the enzyme was reacted with glutaraldehyde to form cross-linked laccase prior to immobilization, and then the cross-linked laccase was entrapped in sodium alginate and gelatin. The main factors affecting the immobilization of cross-linked laccase were investigated. The results showed that the immobilization effect was the best when the mass fraction of glutaraldehyde was 2.0%, the mass ratio of sodium alginate to gelatin was 1∶1 and CaCl2 was 15 g/L. Compared with immobilized free enzyme, the stability of immobilized crosslinked laccase was improved greatly. The degradation experiment of bisphenol A in bubble reactor showed that after five consecutive batches of reaction, the residual enzyme activity of immobilized crosslinking enzyme was 34.93%, and the degradation rate of bisphenol A could still reached 71.13%, which was 7.97 times and 4.43 times higher than that of immobilized free enzyme, respectively. This study provides a new method for immobilization of laccase, which is suitable for repetitive and continuous operation, and has a certain application potential.

Cite this article

WEI Shenghua , SHEN Qi , QIN Mengru , ZHANG Huiyun , TANG Zhongxun , LI Song , MENG Na . Immobilization of cross-linked laccase by sodium alginate-gelatin for degradation bisphenol A in bubbling reactor[J]. Food and Fermentation Industries, 2023 , 49(1) : 140 -145 . DOI: 10.13995/j.cnki.11-1802/ts.031669

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