Isolation and Structural Characterization of Coryxin, a Novel Cyclic Lipopeptide From Corynebacterium Xerosis Ns5 Having Emulsifying and Anti-Biofilm Activity Publisher Pubmed



Dalili D¹ ; Amini M² ; Faramarzi MA³ ; Fazeli MR¹ ; Khoshayand MR¹ ; Samadi N¹
Source: Colloids and Surfaces B: Biointerfaces Published:2015

Abstract

Herein we reported the structure and several properties of a new biosurfactants produced by Corynebacterium xerosis strain NS5. This strain was capable of producing a novel lipopeptide biosurfactant that we have named coryxin. The biosurfactant structure was characterized by using Fourier transform infrared spectroscopy (FTIR), Nuclear magnetic resonance spectroscopy (NMR), and Liquid chromatography-mass spectrometry (LC-MS). It contained a hydrophobic moiety of 3-hydroxydecanoic acid and a peptide part predicted as a sequence of seven amino acids including Asn-Arg-Asn-Gln-Pro-Asn-Ser. Coryxin lowered the surface tension of water to 31.4. mN/m, with a critical micelle concentration of 25 mg/l. It was a strong emulsifier with an emulsification index of 61% against n-hexane. Coryxin showed antibacterial activity against test organisms belonging to Gram-positive and Gram-negative bacteria and disrupted preformed biofilms of Staphylococcus aureus (82.5%). , Streptococcus mutans (80%), Escherichia coli (66%) and Pseudomonas aeruginosa (30%). In conclusion, microbial surfactant from C. xerosis exhibited inhibitory and disruptive activities against biofilm formation that could be of use in biofilm-related menace. © 2015 Elsevier B.V.