Anti-Salmonella Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen (Huso huso) Using Commercial Enzymes

Abstract

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.

Therapeutic Potential of Marine Bioactive Peptides against Human Immunodeficiency Virus: Recent Evidence, Challenges, and Future Trends

“…Additionally, it is often accompanied by a high cost of production, leading to a longer purification process [ 14 , 70 ]. Recent research on antimicrobial marine peptides, or their fractions thereof, are reported to have a molecular weight <10 kDa and a high degree of antimicrobial activity [ 71 ]. Some of the techniques employed for the preparation and purification of MBAPs are listed in Table 1 .…”

Impact of Enzymatic Hydrolysis on Antioxidant Activity of Snakehead Fish (<I>Channa striata</I>) Head Protein Hydrolysate

“…Fish protein hydrolysate (FPH) is a proteinderived substance that has been hydrolyzed to produce amino acid and peptide components of varying molecular sizes. It is widely known to have bioactive peptide with functional properties such as antioxidants (Sohaib et al, 2017;Nurilmala et al, 2020;Shiao et al, 2021), antibacterial (Trang and Pasuwan, 2018;Atef et al, 2021), anti-Inflammatory (Da Rocha et al, 2018), and antihypertensive (Abachi et al, 2019;Naik et al, 2021). Several proteases have been reported to be used for the production of FPH such as orientase, protease XXIII, trypsin, bromelain, papain, protamex, bovine pancreatin 6.0, neutrase 1.5MG, and alcalase (Ren et al, 2007;Hsu, 2010;Šližytė et al, 2016;Yathisha et al, 2022).…”

Collagen-Derived Cryptides: Machine-Learning Prediction and Molecular Dynamic Interaction Against Klebsiella pneumoniae Biofilm Synthesis Precursor

“…The cryptides in collagen hydrolysate have been shown to have angiogenic, mitogenic (Banerjee & Shanthi, 2016), and antibacterial properties ( Ennaas et al, 2016;Atef et al, 2021). The administration of collagen peptides significantly improved exercise-athletic injury pain (Dressler et al, 2018;Zdzieblik et al, 2021) and accelerated healing in patients with Achilles tendonitis (Praet et al, 2019).…”

“…Baehaki et al, (2016) reported that fish skin cryptides produced with bacterial collagenase inhibited angiotensin I-converting enzymes and were anti-cancer. On the other hand, cryptides derived from collagen showed antimicrobial activity against Salmonella spp., Escherichia coli, and Staphylococcus aureus (Atef et al, 2021). However, the antimicrobial potential of collagenderived cryptides still needs to be extensively researched despite the protein diversity from different organisms.…”

“…More than hundreds of collagen proteins curated in the UniProtKB database are potential reservoirs for numerous biologically active cryptides. To date, cryptides have been identified and purified using mass spectrometry to elucidate their function (Baehaki et al, 2016;Ennaas et al, 2016;Atef et al, 2021). However, this approach is expensive, time-consuming, and limited to the characterization of a small number of peptides.…”