“…This indicates that the downstream processing led to the concentration of active peptides in the resulting fraction. Ennaas et al [ 12 ] reported a similar pattern with acetone fractionation of mackerel by-product hydrolysates with antibacterial activity against Gram-positive ( L. innocua ) and Gram-negative bacteria ( E. coli ). The increase in antibacterial activity after fractionation with acetone was attributed to the hydrophobic nature of the fractionated peptides.…”
Section: Discussionmentioning
confidence: 72%
“…Moreover, functional properties of food protein hydrolysates, such as protein solubility, surface hydrophobicity, emulsification, and foaming capacity, depend on the degree of hydrolysis. For instance, the solubility of protein hydrolysate increases with increased DH as observed in samples from yellow stripe trevally [ 35 ], Alaska pollack [ 36 ], barbel [ 13 , 14 ], anchovy [ 37 ], and Atlantic mackerel [ 12 ]. High DH would ensure that the peptides become soluble and accessible to interact with their targets in aqueous physiological environments.…”
Section: Discussionmentioning
confidence: 99%
“…Selected collagen hydrolysates were further subjected to solvent fractionation to separate the bioactive peptides as previously reported [ 12 ]. High-molecular-weight peptides in the samples were precipitated using ice-cold acetone (50%, v/v ) followed by centrifugation at 8000× g for 20 min at 4 °C.…”
Section: Methodsmentioning
confidence: 99%
“…Several studies have reported that treatment of marine organisms by enzymatic hydrolysis yielded AMPs and hydrolysates with activity against pathogenic bacteria. For instance, antibacterial peptide fractions isolated from Atlantic mackerel ( Scomber scombrus ) by-products were reported to inhibit the growth of Gram-positive and Gram-negative bacteria [ 12 ]. Sila et al [ 13 , 14 ] also demonstrated potent inhibitory activity against pathogenic bacteria using antibacterial peptides from barbel muscle protein hydrolysates produced with Alcalase.…”
This study investigated peptide fractions from fish skin collagen for antibacterial activity against Escherichia coli and Salmonella strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight < 10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against E. coli, and Neutrase and papain hydrolysates showing the best activity against S. abony; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four Salmonella strains, including S. abony (NCTC 6017), S. typhimurium (ATCC 13311), S. typhimurium (ATCC 14028) and S. chol (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6–22 and 6–24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure–activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.
“…This indicates that the downstream processing led to the concentration of active peptides in the resulting fraction. Ennaas et al [ 12 ] reported a similar pattern with acetone fractionation of mackerel by-product hydrolysates with antibacterial activity against Gram-positive ( L. innocua ) and Gram-negative bacteria ( E. coli ). The increase in antibacterial activity after fractionation with acetone was attributed to the hydrophobic nature of the fractionated peptides.…”
Section: Discussionmentioning
confidence: 72%
“…Moreover, functional properties of food protein hydrolysates, such as protein solubility, surface hydrophobicity, emulsification, and foaming capacity, depend on the degree of hydrolysis. For instance, the solubility of protein hydrolysate increases with increased DH as observed in samples from yellow stripe trevally [ 35 ], Alaska pollack [ 36 ], barbel [ 13 , 14 ], anchovy [ 37 ], and Atlantic mackerel [ 12 ]. High DH would ensure that the peptides become soluble and accessible to interact with their targets in aqueous physiological environments.…”
Section: Discussionmentioning
confidence: 99%
“…Selected collagen hydrolysates were further subjected to solvent fractionation to separate the bioactive peptides as previously reported [ 12 ]. High-molecular-weight peptides in the samples were precipitated using ice-cold acetone (50%, v/v ) followed by centrifugation at 8000× g for 20 min at 4 °C.…”
Section: Methodsmentioning
confidence: 99%
“…Several studies have reported that treatment of marine organisms by enzymatic hydrolysis yielded AMPs and hydrolysates with activity against pathogenic bacteria. For instance, antibacterial peptide fractions isolated from Atlantic mackerel ( Scomber scombrus ) by-products were reported to inhibit the growth of Gram-positive and Gram-negative bacteria [ 12 ]. Sila et al [ 13 , 14 ] also demonstrated potent inhibitory activity against pathogenic bacteria using antibacterial peptides from barbel muscle protein hydrolysates produced with Alcalase.…”
This study investigated peptide fractions from fish skin collagen for antibacterial activity against Escherichia coli and Salmonella strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight < 10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against E. coli, and Neutrase and papain hydrolysates showing the best activity against S. abony; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four Salmonella strains, including S. abony (NCTC 6017), S. typhimurium (ATCC 13311), S. typhimurium (ATCC 14028) and S. chol (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6–22 and 6–24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure–activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.
“…AMPs have also been identified from Atlantic mackerel after by-product hydrolysis. After purification of hydrolysate generated by the commercial enzyme mixture Protamex ® , four peptide sequences were identified, exhibiting activity against both Gram positive and negative bacteria [14]. Among these peptides, collagencin, identified from the mackerel collagen hydrolysate, was particularly active against Staphylococcus aureus with 67% growth inhibition at 235 µM [15].…”
The Atlantic mackerel, Scomber scombrus, is one of the most fished species in the world, but it is still largely used for low-value products, such as bait; mainly for crustacean fishery. This resource could be transformed into products of high value and may offer new opportunities for the discovery of bioactive molecules. Mackerel hydrolysate was investigated to discover antibacterial peptides with biotechnological potential. The proteolytic process generated a hydrolysate composed of 96% proteinaceous compounds with molecular weight lower than 7 kDa. From the whole hydrolysate, antibacterial activity was detected against both Gram-negative and Gram-positive bacteria. After solid phase extraction, purification of the active fraction led to the identification of 4 peptide sequences by mass spectrometry. The peptide sequence N-KVEIVAINDPFIDL-C, called Atlantic Mackerel GAPDH-related peptide (AMGAP), was selected for chemical synthesis to confirm the antibacterial activity and to evaluate its stability through in vitro digestibility. Minimal inhibitory concentrations of AMGAP revealed that Listeria strains were the most sensitive, suggesting potential as food-preservative to prevent bacterial growth. In addition, in vitro digestibility experiments found rapid (after 20 min) and early digestibility (stomach). This study highlights the biotechnological potential of mackerel hydrolysate due to the presence of the antibacterial AMGAP peptide.
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