Antibacterial activity of new peptide from bovine casein hydrolyzed by a serine metalloprotease of Lactococcus lactis subsp lactis BR16

Bougherra, Fateh; Dilmi-Bouras, Abdelkader; Balti, Rafik; Przybylski, Rémi; Adoui, Faiza; Elhameur, Hacene; Chevalier, Mickaël; Flahaut, Christophe; Dhulster, Pascal; Nedjar, Naïma

doi:10.1016/j.jff.2017.02.026

Cited by 27 publications

(18 citation statements)

References 52 publications

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“…Lactobacillus kefiranofaciens subsp. kefiranofaciens is a microorganism primarily responsible for the production of kefiran, a water-soluble polysaccharide in which the kefir grain microbial consortium is embedded and that has been reported as having antibacterial, antitumoral and antidiabetic properties, as well as several technological roles as a thickener, gelling agent and emulsifier [2,13] Similar studies on cow's milk were performed by Bougherra et al [4]. Researchers analysed antibacterial properties against E. coli, Salmonella enteritidis, Micrococcus luteus [11] studied the antibacterial activity of Lactobacillus rhamnosus using nine pathogenic bacteria, both Gram (−) and Gram ( +), aerobes and anaerobes.…”

Section: Resultsmentioning

confidence: 74%

Antimicrobial activity of goat’s milk fermented by single strain of kefir grain microflora

Biadała

Szablewski

Lasik-Kurdyś

et al. 2020

Eur Food Res Technol

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The aim of the study was to assess the antibacterial properties of bioactive compounds released during the fermentation of goat's milk by selected bacterial strains that are part of the kefir grain microflora. The material used in the experiments was kefir grain microflora (Lactobacillus kefiranofaciens subsp. kefirgranum DSM 10550, Lactobacillus kefiri PCM 2501, Lactobacillus parakefiri DSM 10551, Lactobacillus brevis PCM 488, Lactobacillus delbrueckii subsp. lactis PCM 2611), goat's and cow's milk and whey from these kinds of milk. The antimicrobial activity was tested against E. coli, Salmonella, Micrococcus luteus and Proteus mirabilis. Based on the experiments, it was found that during the fermentation of whey and goat's milk, bioactive substances were released, which inhibit the growth of indicator microorganisms by up to 8 logarithmic cycles.

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Section: Resultsmentioning

confidence: 74%

Antimicrobial activity of goat’s milk fermented by single strain of kefir grain microflora

Biadała

Szablewski

Lasik-Kurdyś

et al. 2020

Eur Food Res Technol

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“…Finally, Lactococcus lactis subsp. lactis BR16 was found to hydrolyze bovine casein through the secretion of extracellular serine metalloproteases, generating a new antibacterial peptide from αs2-casein corresponding to the fragment (24–31; Bougherraa et al, 2017 ).…”

Section: Discussionmentioning

confidence: 99%

Two New Secreted Proteases Generate a Casein-Derived Antimicrobial Peptide in Bacillus cereus Food Born Isolate Leading to Bacterial Competition in Milk

et al. 2018

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Milk and dairy products harbor a wide variety of bacterial species that compete for both limited resources and space. Under these competitive conditions, bacteria develop specialized mechanisms to protect themselves during niche colonization and nutrient acquisition processes. The bacterial antagonism mechanisms include the production of antimicrobial agents or molecules that facilitate competitor dispersal. In the present work, a bacterial strain designated RC6 was isolated from Ricotta and identified as Bacillus cereus. It generates antimicrobial peptide (AMP) when grown in the presence of casein. The AMP was active against several species of Bacillus and Listeria monocytogenes. MALDI-TOF analysis of the RP-HPLC purified fractions and amino acid sequencing revealed a molecular mass of 751 Da comprised of a 6-residue sequence, YPVEPF. BLAST analysis showed that the AMP corresponds to the fractions 114–119 of bovine β-casein and represents the product of a specific proteolysis. Analysis of the purified proteolytic fractions from the B. cereus RC6 culture supernatant indicated that the presence of at least two different endoproteases is crucial for the generation of the AMP. Indeed, we were able to identify two new candidate endoproteases by means of genome sequencing and functional assignment using a 3D structural model and molecular docking of misannotated hypothetical proteins. In this light, the capacity of B. cereus RC6 to generate antimicrobial peptides from casein, through the production of extracellular enzymes, presents a new model of antagonistic competition leading to niche colonization. Hence, as a dairy product contaminant, this strategy may enable proteolytic B. cereus RC6 niche specialization in milk matrices.

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“…In addition to the active peptides, the total hydrolysate contains a large number of peptides without antimicrobial activity (Bougherra et al, 2017). The method of live E. coli affinity adsorption was used to selectively absorb the AMP contained in the hydrolysate, which avoided cumbersome separation methods (e.g., ion exchange, gel filtration, liquid chromatography).…”

Section: Selective Separation Of Amp By Live E Coli Adsorptionmentioning

confidence: 99%

“…Antimicrobial peptides penetrate the outer membranes of gram-negative bacteria and the cell walls of gram-positive bacteria, creating holes that lead to leakage of intracellular contents (López-Expósito and Recio, 2008). Most AMP have helical, amphipathic, and hydrophobic structures, with positive charge (Bougherra et al, 2017). In general, it is suggested that peptide drugs exhibit lower toxicity and higher specificity and are more easily synthesized and modified than nonpeptide drugs; thus they have great potential for control of bacterial contamination (Lombardi et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel antimicrobial peptide from buffalo casein hydrolysate based on live bacteria adsorption

Zhao

Shi

Wang

et al. 2020

Journal of Dairy Science

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This study aims to isolate the antimicrobial peptide (AMP) from buffalo casein hydrolyzed by Dregea sinensis Hemsl. protease. The AMP was isolated from hydrolysate by live bacteria adsorption, then analyzed using reversed-phase high-performance liquid chromatography, and the fraction with highest antimicrobial activity was identified by liquid chromatography-tandem MS. Further, we characterized the peptide in terms of its peptide sequence, structure, and antimicrobial activity. The results identified the AA sequence of the peptide as YLGYLEQLLRLK, which corresponds to residues 106 to 117 of bovine α S1-casein, and we named it BCp12. BCp12 displays α-helical structure, with high hydrophobic moments and net positive charge. BCp12 can inhibit the growth of indicator bacteria, with minimum inhibitory concentration values ranging from 0.8 to 1.6 mg/mL, and can induce low toxicity in mammalian cells. Antimicrobial activity of the BCp12 peptide remained stable under different salt concentrations but was sensitive to trypsin and high temperatures (121°C and above). The results support further research in the application of our newly generated AMP as an antimicrobial agent in the food industry and in food processing facilities.

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Antibacterial activity of new peptide from bovine casein hydrolyzed by a serine metalloprotease of Lactococcus lactis subsp lactis BR16

Cited by 27 publications

References 52 publications

Antimicrobial activity of goat’s milk fermented by single strain of kefir grain microflora

Antimicrobial activity of goat’s milk fermented by single strain of kefir grain microflora

Two New Secreted Proteases Generate a Casein-Derived Antimicrobial Peptide in Bacillus cereus Food Born Isolate Leading to Bacterial Competition in Milk

Characterization of a novel antimicrobial peptide from buffalo casein hydrolysate based on live bacteria adsorption

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