Abstract
Objective: This study explores the sustainable valorization of by-products from tuna fish based on in silico approach.
 Methods: In silico approaches (BIOPEP database, PeptideRanker database, peptide calculator [PepCalc] database, and toxin prediction [ToxinPred] database) were employed to evaluate the potential of collagens from tuna as a potential source of bioactive peptides. Furthermore, primary structure, biological potential, physicochemical, sensory, and toxicity characteristics of the theoretically released angiotensin-converting enzyme (ACE) inhibitor collagen peptides were predicted.
 Results: Tuna collagen was selected as a potential precursor of bioactive peptides based on in silico analysis. Most notable among these are ACE inhibitory peptides. First, the potential of tuna collagen for the releasing bioactive peptides was evaluated by determining the frequency of occurrence of fragments with a given activity. Through the BIOPEP database analysis, there are many bioactive peptides in tuna collagen sequences. Then, an in silico proteolysis using selected enzymes (papain and pepsin) to obtained ACE inhibitory peptides was investigated and then analyzed using PeptideRanker and PepCalc. Cytotoxicity analysis using the online toxic prediction tool ToxinPred revealed that all in silico proteolysis-derived ACE inhibitory peptides are non-cytotoxic.
 Conclusions: Overall, the present study highlights that the tuna collagens could be a promising precursor of bioactive peptides that have an antihypertensive effect (ACE inhibitory activities) for developing functional food or nutraceutical products.
Highlights
Fish skin gelatin is extensively employed as an ingredient to improve the elasticity, consistency, and stability of foods, but it can be a source of collagen
Incorporation of collagen-derived bioactive compounds can be an innovative approach to the production of functional food and nutraceutical products with potential health-promoting properties [1,4]
Collagen type I-1 protein sequences were subjected to in silico proteolysis to predict the theoretical peptide sequences cleaved by enzyme mixture [1]
Summary
Fish skin gelatin is extensively employed as an ingredient to improve the elasticity, consistency, and stability of foods, but it can be a source of collagen. Collagen and its derivatives have potential commercial value for a broad application range of pharmaceutical, cosmetic, food, and biomedical industry applications [1,2]. The skin and bone of land-based animals (bovine and porcine) have been the conventional sources of collagen [2,3]. The use of bovine and porcine collagens has raised serious problems regarding consumers’ health [2,3]. There is a strong necessity nowadays to find the alternative sources of collagen. Incorporation of collagen-derived bioactive compounds can be an innovative approach to the production of functional food and nutraceutical products with potential health-promoting properties [1,4]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Asian Journal of Pharmaceutical and Clinical Research
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
