FOOD SCIENCE ›› 2011, Vol. 32 ›› Issue (15): 182-185.doi: 10.7506/spkx1002-6630-201115041

• Bioengineering • Previous Articles     Next Articles

Effect of Disulfide Bond on Anti-Listeria innocua LIN3 Activity of Enterocin A

ZHAO Ai-zhen1,XU Xing-ran1,HAN Wen-yu2   

  1. (1. College of Pharmaceutical Sciences, Southwest University, Chongqing 400715, China; 2. College of Animal Science and Veterinary Medicine, Jilin University, Changchun 130062, China)
  • Received:2018-04-20 Revised:2018-04-20 Online:2011-08-15 Published:2011-07-26

Abstract: Based on the amino acid sequence of Enterocin A, two cysteine substitution mutants, Enterocin A (C14S) and Enterocin A (C47W) were designed and obtained in E. coli expression systems. The agar diffusion assay was used to test the anti-Listeria innocua LIN3 activity of the mutants, recombinant Enterocin A and β-mercaptoethanol-reduced recombinant Enterocin A. Recombinant Enterocin A with His-tag at N-terminus revealed stronger antibacterial activity, while GST-Enterocin A revealed a significant decrease in antibacterial activity. The two mutants andβ-mercaptoethanol-reduced recombinant Enterocin A with destroyed disulfide bonds exhibit no detectable antibacterial activity. Therefore, disulfide bonds are essential for the antibacterial activity of Enterocin A.

Key words: Enterocin A, disulfide bond, anti-Listeria activity

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