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Published on: September 19, 2022
Purification and partial chemical characterization of the antimicrobial peptide cerein 8A
D Bizani1, A P M Dominguez, A Brandelli
1Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de Alimentos, ICTA, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil.
Aims:
To purify and to characterize the antimicrobial compound cerein 8A.
Methods And Results:
Cerein 8A was isolated by ammonium sulfate precipitation, 1-butanol extraction and ion-exchange chromatography. Direct activity on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was observed. The purified substance corresponded to a 26 kDa peptide band. The native protein eluted at the void volume of Sephadex G-100, but within the included volume when a 1.5 mol l(-1) NaCl buffer was used, indicating that cerein 8A aggregates extracellularly. The antimicrobial activity was lost by treatment with proteases and heat. The ultraviolet spectrum was typical of a polypeptide and the infrared spectrum indicates that the peptide contains acyl group(s) in its structure. Intact Bacillus cereus spores were sensitive to cerein 8A at 1600 AU ml(-1).
Conclusions:
Cerein 8A show distinct properties from other antimicrobial peptides of B. cereus, and has a significant inhibitory effect on spores.
Significance And Impact Of The Study:
The characterization of a substance active against important pathogens addresses an important aspect of food safety.
