Literature DB >> 7763922

Isolation and physico-chemical characterization of an antifungal and antibacterial peptide produced by Bacillus licheniformis A12.

A Gálvez1, M Maqueda, M Martínez-Bueno, M Lebbadi, E Valdivia.   

Abstract

An antifungal substance named peptide A12-C has been purified to homogeneity from supernatants of sporulated cultures of Bacillus licheniformis A12. It consists of a 0.77-kDa hydrophilic peptide containing two residues of Glu and one of Arg, Ala, Pro, Tyr and Orn. No fatty acids, phosphorus or carbohydrates have been detected. Peptide A12-C is active on several fungi (Microsporum canis CECT 2797, Mucor mucedo CECT 2653, M. plumbeus (CCM F 443, Sporothrix schenckii CECT 2799 and Trichophyton mentagrophytes CECT 2793) and bacteria (Bacillus megaterium, Corynebacterium glutamicum, Sarcina and Mycobacterium), although the latter are less sensitive.

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Year:  1993        PMID: 7763922     DOI: 10.1007/BF00205029

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  3 in total

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Authors:  E Katz; A L Demain
Journal:  Bacteriol Rev       Date:  1977-06

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3.  Studies on the biosynthesis of surfactin, a lipopeptide antibiotic from Bacillus subtilis ATCC 21332.

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