Keywords

Brevibacillus, Laterosporus, Polypeptides, Properties, Mechanism Of Action

Abstract

The properties and mechanism of action of polypeptide R-1 produced by Brevibacillus laterosporus Lh-1 were studied. R-1 is stable to temperature and pH. Under pH conditions of 11.0 to 12, its activity remains above 75% after treatment at 121¡ãC for 1 hour. After being treated with three different concentrations of proteases (alkaline protease, trypsin, pepsin) for 4 hours, the activity remained above 80%. It reacts with common metal ions and chemical reagents and has no significant impact on the activity of antimicrobial peptide R-1. It can be used together. Only Tween and SDS have a greater impact on it. Amino acid analysis showed that antimicrobial peptide R-1 consists of leucine (Leu), tyrosine (Tyr), valine (Val), isoleucine (Ile), lysine (Lys), and glycine (Gly). It is composed of 9 amino acids, methionine (Met), serine (Ser), and alanine (Ala), among which hydrophobic amino acids are the majority. Antibacterial tests show that R-1 has a broad antibacterial spectrum. Scanning electron ultrastructural observations of Escherichia coli and Candida albicans isolated after culture showed that the bactericidal mechanism of R-1 is mainly through containing positively charged substances. Lys binds to the negatively charged phospholipid molecules, and then the hydrophobic end of R-1 is inserted into the hydrophobic region of the indicator bacteria, changing the conformation of the membrane, resulting in the death of the bacteria.

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Original research done by Ren Zhaozhen, Sun Mi, Zheng Yuan, Liu Junzhong, Wang Yuejun, Hao Jianhua, Zhang Shengjun

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