Expression and Purification of Multimeric Natto Peptide in Escherichia coli and Initial Characterization of Its Antimicrobial Activity and Stability

• 作者: Bin DONG
• 来源期刊: 农业生物技术:英文版
• 学科: 化学
• 关键词: ANTIMICROBIAL PEPTIDE ANTIMICROBIAL activity ESCHERICHIA COLI Heterogenous expression NATTO PEPTIDE
• 年，卷（期）: 2020,（1）
• 页码范围: 9-11
• 页数: 3页
• 分类号: O62

摘要

Increasing amounts of antibiotic resistant bacteria have been an emergency problem. Antimicrobial peptides are promising antibiotic alternatives for broad-spectrum antimicrobial activity and nearly no drug resistance. Natto peptide was a new antimicrobial peptide which consisted of 45 amino acids. In this study, to improve the antimicrobial activity of Natto peptide, three repeats of encoding sequences were synthesized and cloned into a pET28 a(+) expression vector, and expressed in Escherichia coli as a soluble protein. Unexpectedly, the purified 3×Natto peptide exhibited antimicrobial activity against Listeria monocytogenes(50 μg/ml) and Salmonella enteriditis(30 μg/ml). Furthermore, the antibacterial spectrum of 3×Natto peptide was not affected by temperature, pH value and proteinase digestion. Taken together, this was the first study proving that 3×Natto peptide could be produced in E. coli as a kind of water dissolve protein, and has great potential for commercial application in the future.