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

作　　者：Bin DONG 

机构地区：[1]Shandong Provincial Engineering and Technology Research Center for Wild Plant Resources Development and Application of Yellow River Delta,College of Biological and Environmental Engineering,Binzhou University

出　　处：《Agricultural Biotechnology》2020年第1期9-11,113,共4页农业生物技术（英文版）

基　　金：Supported by Shandong Provincial Natural Science Foundation(ZR2018PC010);the Doctor Foundation of Binzhou University(2018Y09);Natural Science Program of Binzhou University(BZXYG1811)

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.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.

关 键 词：Antimicrobial peptide Antimicrobial activity Escherichia coli Heterogenous expression Natto peptide 

分 类 号：Q93[生物学—微生物学]