Antioxidant peptides generated from chicken feet protein hydrolysates

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dc.authoridOzturk Kerimoglu, Burcu/0000-0001-9777-8510
dc.authorscopusid57210432767
dc.authorscopusid57201897014
dc.authorscopusid14123757700
dc.authorscopusid7005015097
dc.authorwosidOzturk Kerimoglu, Burcu/AFP-2897-2022
dc.contributor.authorOzturk-Kerimoglu, Burcu
dc.contributor.authorHeres, Alejandro
dc.contributor.authorMora, Leticia
dc.contributor.authorToldra, Fidel
dc.date.accessioned2024-08-25T18:31:53Z
dc.date.available2024-08-25T18:31:53Z
dc.date.issued2023
dc.departmentEge Üniversitesien_US
dc.description.abstractBackgroundAs major industrial poultry by-products, chicken feet are considered as notable sources of several bioactive molecules. The current work covers the processing of chicken feet proteins as substrates to be hydrolysed by combinations of three commercial enzymes (Alcalase & REG;, Flavourzyme & REG; and Protana & REG; Prime) during different hydrolysis periods and the evaluation of the identified peptides having antioxidant activity after simulated gastrointestinal digestion. ResultsEnzymatic hydrolysis with Alcalase & REG; and Protana & REG; Prime combination for 4 h resulted in the highest activities. Reversed-phase high-performance liquid chromatographic separation of the purified hydrolysate yielded three active fractions that were further identified by nano-liquid chromatography-tandem mass spectrometry. The bioactivities of over 230 identified peptide sequences were estimated after simulated gastrointestinal digestion, and those peptides with the highest chance of exerting antioxidant activity were selected to be further synthesised and tested. In this sense, the synthesised dipeptides CF and GY showed the highest antioxidant capacity. CF presented IC50 values of 69.63 and 145.41 & mu;mol L-1 in 2,2 & PRIME;-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and oxygen radical absorbance capacity (ORAC) assays, respectively. In contrast, GY IC50 values were 15.27 and 10.06 & mu;mol L-1 in ABTS and ORAC assays, respectively. Significant differences (P < 0.05) were registered between peptides in the same antioxidant assays. ConclusionOverall, the findings emphasised the favourable impact of enzymatic hydrolysis with the obtaining of antioxidant peptides from poultry by-products that could be evaluated as a safe and economical source to retard oxidation in food systems. & COPY; 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.en_US
dc.description.sponsorshipScientific and Technological Research Council of Tuerkiye (TUEBITAK) Science Fellowships and Grant Programs Directorate within the Post-Doctoral Fellowship 2219 Program [PID2020-119684RB-I00, MCIN/AEI/10.13039/501100011033]en_US
dc.description.sponsorship& nbsp;Grant PID2020-119684RB-I00 funded by MCIN/AEI/10.13039/501100011033 is acknowledged. Dr. Ozturk-Kerimoglu gratefully acknowledges the financial support of the Scientific and Technological Research Council of Tuerkiye (TUEBITAK) Science Fellowships and Grant Programs Directorate within the Post-Doctoral Fellowship 2219 Program. The authors are also grateful to PhD students Ms Gisela Carrera Alvarado, Mr Chengliang Li and Ms Aleksandra Purkiewicz for their kind assistance throughout the laboratory work.en_US
dc.identifier.doi10.1002/jsfa.12802
dc.identifier.issn0022-5142
dc.identifier.issn1097-0010
dc.identifier.pmid37347843en_US
dc.identifier.scopus2-s2.0-85164466658en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1002/jsfa.12802
dc.identifier.urihttps://hdl.handle.net/11454/100055
dc.identifier.wosWOS:001023470400001en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofJournal of The Science of Food and Agricultureen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.snmz20240825_Gen_US
dc.subjectenzymatic hydrolysisen_US
dc.subjectbioactive peptideen_US
dc.subjectantioxidant peptideen_US
dc.subjectpoultry protein hydrolysateen_US
dc.subjectanimal by-productsen_US
dc.subjectIn-Vitro Antioxidanten_US
dc.subjectBioactive Peptidesen_US
dc.subjectMilken_US
dc.titleAntioxidant peptides generated from chicken feet protein hydrolysatesen_US
dc.typeArticleen_US

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