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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Correspondence to: A. Gálvez
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Gálvez, A., Maqueda, M., Martínez-Bueno, M. et al. Isolation and physico-chemical characterization of an antifungal and antibacterial peptide produced by Bacillus licheniformis A12. Appl Microbiol Biotechnol 39, 438–442 (1993). https://doi.org/10.1007/BF00205029
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DOI: https://doi.org/10.1007/BF00205029