ArticleWorld journal of microbiology & biotechnology2021
In vitro and in silico approach for characterization of antimicrobial peptides from potential probiotic cultures against Staphylococcus aureus and Escherichia coli.
Article in World journal of microbiology & biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Promising Future of Engineered Probiotics for Antimicrobial Peptides and Protein Production: Prospects and Industrial Challenges.Probiotics and antimicrobial proteins · 2026Review
- Antimicrobial peptides isolated from probiotics as an alternative to antibiotics againstApplied and environmental microbiology · 2026Article
- Bactericidal and cell membrane disruption potential of protein extract from buttermilk-derived probioticFrontiers in microbiology · 2026Article
- Biopreservation strategies using bacteriocins to control meat spoilage and foodborne outbreaks.Italian journal of food safety · 2024Review
- Metabolite profiling and bioactivity guided fractionation ofFrontiers in microbiology · 2024Article
- Genetic and phenotypic assessment of the antimicrobial activity of three potential probiotic lactobacilli against human enteropathogenic bacteria.Frontiers in cellular and infection microbiology · 2023Article
- Identification and characterization of probiotics isolated from indigenous chicken (Gallus domesticus) of Nepal.PloS one · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The focus of the present study was to characterize antimicrobial peptide produced by potential probiotic cultures of Enterococcus durans DB-1aa (MCC4243), Lactiplantibacillus plantarum Cu2-PM7 (MCC4246) and Limosilactobacillus fermentum Cu3-PM8 (MCC4233) against Staphylococus aureus MTCC 96 and Escherichia coli MTCC118. The growth kinetic assay revealed 24 h of incubation to be optimum for bacteriocin production. The partially purified compound of all the three selected cultures after ion-exchange chromatography was found to be thermoresistant and stable under a wide range of pH. The compound was sensitive to proteinase-K, but resistant to trypsin, α-amylase and lipase. Comparatively, bacteriocins from L. fermentum Cu3-PM8 and L. plantarum Cu2-PM7 showed higher stability under studied parameter, hence was taken up for further investigation. The apparent molecular weight of bacteriocin from L. fermentum MCC4233 and L. plantarum MCC4246 was found to be 3.5 kDa. Further, plantaricin gene from MCC4246 was characterized in silico. The translated partial amino acid sequence of the plnA gene in MCC4246 displayed 48 amino acids showing 100 % similarity with plantaricin A of Lactobacillus plantarum (WP_0036419). The sequence revealed 7 β sheets, 6 α sheets, 6 predicted coils and 9 predicted turns. The predicted properties of the peptide included an isoelectric point of 10.82 and a hydrophobicity of 48.6 %. The molecular approach of using Geneious Prime software and protein prediction data base for characterization of bacteriocin is novel and predicts "KSSAYSLQMGATAIKQVKKLFKKWGW" to be a peptide responsible for antimicrobial activity. The study provides information about a broad spectrum bacteriocin in native probiotic culture and paves a way towards its application in functional foods as a biopreservative agent.
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