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Updated: Jul 16, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Purification and partial characterization of an antimicrobial peptide produced by a novel Bacillus sp. isolated from
Amanda S Motta1, Daniel M Lorenzini, Adriano Brandelli
1Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência dos Alimentos, ICTA, Universidade Federal do Rio Grande do Sul, Av Bento Gonçalves 9500, 91501-970, Porto Alegre, Brazil.
Abstract:
An antimicrobial peptide produced by a new Bacillus species isolated from the Amazon Basin was purified and characterized. The antimicrobial peptide was purified by ammonium sulfate precipitation, gel filtration, and ion exchange chromatography, and after the final purification step, one active fraction was obtained, designated BLS P34. Direct activity on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was observed. A single band on SDS-PAGE suggested that the peptide was purified to homogeneity and had a molecular mass of about 5 kDa. The molecular weight (MW) was accurately determined by mass spectroscopy as 1456 Da. The purified BLS P34 remained active over a wide temperature range and was susceptible to all proteases tested.
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