Comparative Studies concerning Bioactive Peptides Obtained from Fish By-Products †
by
Agnes Toma
*, 
Simona Savin
,
Teodora Ciucan
,
Elena Mihai
,
Catalina Sanda
,
Lucia Moldovan
and
Anca Oancea
National Institute R&D for Biological Sciences, 296, Splaiul Independentei, 060031 Bucharest, Romania
*
Author to whom correspondence should be addressed.
†
Presented at the 17th International Symposium “Priorities of Chemistry for a Sustainable Development” PRIOCHEM, Bucharest, Romania, 27–29 October 2021.
Chem. Proc. 2022, 7(1), 62; https://doi.org/10.3390/chemproc2022007062
Published: 6 April 2022
(This article belongs to the Proceedings of The 17th International Symposium “Priorities of Chemistry for a Sustainable Development” PRIOCHEM)
Fish byproducts (bone, scale, or skin) contain a wide range of nutritional components, especially proteins and lipids, the most important of all being collagen. The hydrolysate of collagen from this source, obtained by the enzymatic method with papain, is rich in bioactive peptides.The aim of this work was to obtain and characterize peptides obtained by enzymatic hydrolysis from fish byproducts. Collagen was obtained by enzymatic methods with pepsin. Peptides were obtained from extracted collagen by enzymatic hyrolysis with papain and were separated by tangential ultrafiltration (using ÄKTA flux cross flow filtration system). This method allowed the separation of low molecular weight peptides (1–30 kDa) from those with high molecular weight (>50 kDa). Bovine collagen hydrolyzate was used as a control. For the peptide samples, we determined: protein content (by Biuret method), antioxidant capacity (by DPPH and ABTS methods), protein hydrolysis degree (using 2,4,6-trinitrobenzenesulfonic acid-TNBS reagent [1]), the inhibitory potential of angiotensin converting enzyme (ACE) [2] and the cytotoxicity in NCTC fibroblast cell line (clone L929) according to the international standard SR EN ISO 10993-5, by MTT assay. SDS-Page electrophoresis was used to assess the presence of peptides in the mass range of 1–100 kDa [3]. The results obtained for the hydrolysis degree as well as for the ultrafiltrated peptides were confirmed by the electrophoresis profile. Biochemical determinations (the antioxidant capacity, the ACE inhibition potential) and the cytotoxicity of tested peptides, with MW lower than 50 kDa, demonstrated their bioactivity. The results of the MTT assay demonstrated that obtained peptides did not affect the cell viability in the range of concentration 50–1000 µg/mL, except bovin collagen sample which is slightly cytotoxic at 1000 µg/mL concentration. Our results showed that the collagen peptides obtained after fish collagen hydrolysis with papain had antioxidant and antihypertensive activity, and the treatment of NCTC fibroblast cells with these peptides did not affect the cell viability. These results suggest that peptides obtained by enzymatic hydrolysis from freshwater fishes by-products collagen can be used in food supplements or cosmetic products.
Author Contributions
Conceptualization, data curation, writing—review and editing, and funding acquisition, A.T. and L.M.; resources, formal analysis, investigation and writing—original draft preparation, E.M., T.C., C.S., S.S., A.T. and A.O. All authors have read and agreed to the published version of the manuscript.
Funding
This research was financially supported by the project PN-III-CERC-CO-PTE-2-2019 3PTE (COLSTIM) 2020–2022.
Institutional Review Board Statement
Not applicable.
Informed Consent Statement
Not applicable.
Data Availability Statement
Not applicable.
Conflicts of Interest
The authors declare no conflict of interest.
References
- Adler-Nissen, J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 1979, 27, 1256–1262. [Google Scholar] [CrossRef] [PubMed]
- Papadimitriou, C.G.; Vafopoulou-Mastrojiannaki, A.; Silva, S.V.; Gomes, A.M.; Malcata, F.X.; Alichanidis, E. Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity. Food Chem. 2012, 105, 647–656. [Google Scholar] [CrossRef]
- Schägger, H.; von Jagow, G. Tricine–sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1–100 kD. Anal. Biochem. 1987, 166, 368–379. [Google Scholar] [CrossRef]
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MDPI and ACS Style
Toma, A.; Savin, S.; Ciucan, T.; Mihai, E.; Sanda, C.; Moldovan, L.; Oancea, A. Comparative Studies concerning Bioactive Peptides Obtained from Fish By-Products. Chem. Proc. 2022, 7, 62. https://doi.org/10.3390/chemproc2022007062
AMA Style
Toma A, Savin S, Ciucan T, Mihai E, Sanda C, Moldovan L, Oancea A. Comparative Studies concerning Bioactive Peptides Obtained from Fish By-Products. Chemistry Proceedings. 2022; 7(1):62. https://doi.org/10.3390/chemproc2022007062
Chicago/Turabian StyleToma, Agnes, Simona Savin, Teodora Ciucan, Elena Mihai, Catalina Sanda, Lucia Moldovan, and Anca Oancea. 2022. "Comparative Studies concerning Bioactive Peptides Obtained from Fish By-Products" Chemistry Proceedings 7, no. 1: 62. https://doi.org/10.3390/chemproc2022007062
