Prokaryotic expression and functional analysis of linoleic acid isomerase from Bifidobacterium breve

  • JI Yibin ,
  • MEI Yongchao ,
  • YANG Bo ,
  • CHEN Haiqin
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  • (School of Food Science and Technology, Jiangnan University, Wuxi 214122, China)

Received date: 2023-02-06

  Revised date: 2023-02-27

  Online published: 2024-01-02

Abstract

Bifidobacterium breve isomerase(BBI), the linoleic acid isomerase from Bifidobacterium breve CCFM683, is the only known single enzyme from lactic acid bacteria that catalyzes the formation of linoleic acid into cis9, trans11-CLA. Using pET-28a(+) as expression vector to construct recombinant vectors pET-28a(+)-bbi-His and pET-28a(+)-His-bbi with His-tag located at C-terminal and N-terminal, which was heterologous expressed in Escherichia coli BL21(DE3), E. coli BL21(DE3) pLysS and E. coli Rosetta(DE3) respectively. The optimum inductive condition for BBI expression is E. coli Rosetta/pET-28a(+)-bbi-His under the induction of 1.0 mmol/L IPTG for 8 h. BBI prefers α-linolenic acid to linoleic acid and γ-linolenic acid when it catalyzed fatty acid.

Cite this article

JI Yibin , MEI Yongchao , YANG Bo , CHEN Haiqin . Prokaryotic expression and functional analysis of linoleic acid isomerase from Bifidobacterium breve[J]. Food and Fermentation Industries, 2023 , 49(23) : 64 -69 . DOI: 10.13995/j.cnki.11-1802/ts.035035

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