Journal
FOOD CHEMISTRY
Volume 425, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2023.136454
Keywords
Casein antimicrobial peptide; Oral pathogenic bacteria; Proteolysis in vitro; Proteomic analysis
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In this study, active casein antimicrobial peptide (CAMPs) mixtures with high antimicrobial activity against Streptococcus mutans and Porphyromonas gingivalis were generated through optimized proteolytic cleavage of milk casein. The CAMPs mixtures also effectively inhibited microbial biofilm attachment and development. Unbiased proteomic analysis identified 301 potential CAMPs sequences, and 4 novel CAMPs were successfully confirmed using synthetic standards. This study provides a promising milk CAMPs resource for the development of safe agents against oral bacteria and functional foods.
Milk casein is a rich source of antimicrobial peptides (AMPs) and the most common way to produce AMPs is enzymatic hydrolysis in vitro. In this study, active casein antimicrobial peptide (CAMPs) mixtures were generated by optimized proteolytic cleavage of milk casein. These natural-safe CAMPs mixtures exhibited high activity in the inhibition of Streptococcus mutans and Porphyromonas gingivalis. Morphological characterization suggested the pathogenic bacteria presented incomplete or irregular collapsed membrane surface after the treatment with active CAMPs mixtures. The CAMPs inhibition activity was also effective in the attachment and development of microbial biofilm. Potential CAMPs sequences were unambiguously determined by unbiased proteomic analysis and 301 potential CAMPs were obtained. The activity of 4 novel CAMPs was successfully confirmed by using synthetic standards. This study provides a promising milk CAMPs resource for the development of safe agents in oral bacteria inhibition and functional foods.
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