Studies on enzymatic characteristics and esterification ability of acid lipase Tgl from Aspergillus niger

  • LI Wenyao ,
  • CHEN Feifan ,
  • ZHENG Jia ,
  • LIU Yining ,
  • DU Liping ,
  • LU Yanping ,
  • MA Lijuan
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  • 1(College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China)
    2(Yibin Wuliangye Group Co., Ltd., Yibin 644000, China)

Received date: 2023-06-05

  Revised date: 2023-07-04

  Online published: 2024-06-11

Abstract

Lipase is a biocatalyst with multiple catalytic capacity such as hydrolysis, esterification, and transesterification.To study the esterification ability of lipase, the gene encoding lipase Tgl from Aspergillus niger was cloned and expressed, and the structure, enzymatic characteristics as well as the esterification ability to synthesize fatty acid ethyl ester of Tgl were studied in this work.Results showed that the optimal reaction temperature of Tgl was 50 ℃, and the residual enzyme activity was about 70% after incubation at 50 ℃ for 12 h.The optimal reaction pH of Tgl was 5.0, and the relative enzyme activity was about 70% after incubation at pH 5.0 for 12 h. Organic reagents showed different degrees of inhibition on Tgl, among which ethanol had the most obvious inhibitory effect on Tgl, but the residual enzyme activity of Tgl was still close to 80% under 40% ethanol system.In 20% ethanol system, the yield of ethyl acetate (41.62 mg/L) catalyzed by Tgl was the highest, while that of ethyl hexanoate was the highest, up to 171.08 mg/L, in 60% ethanol system.In conclusion, acid lipase Tgl from A.niger had high ability to catalyze the synthesis of fatty acid ethyl ester, which would have great application potential in brewing industry.

Cite this article

LI Wenyao , CHEN Feifan , ZHENG Jia , LIU Yining , DU Liping , LU Yanping , MA Lijuan . Studies on enzymatic characteristics and esterification ability of acid lipase Tgl from Aspergillus niger[J]. Food and Fermentation Industries, 2024 , 50(10) : 237 -243 . DOI: 10.13995/j.cnki.11-1802/ts.036366

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