Jairo Andrés Camaño
Echavarría*, Rachel Irankunda, Philippe Arnoux, Christelle Mathé, Jean-Michel Girardet, Céline Cakir-Kiefer, Arnaud Risler, Loïc Stefan, Cédric Paris, José Edgar Zapata Montoya, Katalin Selmeczi and Laetitia Canabady-Rochelle*,
{"title":"Characterization and Bioactivities of Gelatin Hydrolysates of Red Tilapia (Oreochromis spp.) Scale Byproducts","authors":"Jairo Andrés Camaño\r\nEchavarría*, Rachel Irankunda, Philippe Arnoux, Christelle Mathé, Jean-Michel Girardet, Céline Cakir-Kiefer, Arnaud Risler, Loïc Stefan, Cédric Paris, José Edgar Zapata Montoya, Katalin Selmeczi and Laetitia Canabady-Rochelle*, ","doi":"10.1021/acsfoodscitech.4c0091810.1021/acsfoodscitech.4c00918","DOIUrl":null,"url":null,"abstract":"<p >This study explores the production of gelatin hydrolysates with metal-chelating peptides derived from red tilapia scales and investigates their biofunctional properties. Gelatin was enzymatically hydrolyzed using Alcalase (Alc-GH), Flavourzyme (Flav-GH), or a sequential combination of Alcalase and Flavourzyme (Alc+Flav-GH). Alc-GH and Alc+Flav-GH were ultrafiltrated at 1 kDa cutoff. Alc+Flav-GH, characterized by a high proportion of small-sized peptides, exhibited superior metal-chelating ability, as determined by switchSENSE and was associated with enhanced antioxidant activity. Ultrafiltration improved the Fe<sup>2+</sup>-chelating properties of both fractions compared to their respective whole hydrolysates. All of the hydrolysates and their ultrafiltrates showed remarkable ACE inhibitory activity. Specifically, the ≤1 kDa Alc-GH fraction produced small-sized Fe<sup>2+</sup>-chelating peptides with ACE inhibitory activity, whereas the ≤1 kDa Alc+Flav-GH fraction efficiently generated Ni<sup>2+</sup>-chelating peptides with strong antioxidant potential. LC-MS/MS data showed peptides rich in Asp, Glu, Ser, Lys, and Arg, which may contribute to their metal-chelating and antioxidant properties.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1100–1115 1100–1115"},"PeriodicalIF":2.6000,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS food science & technology","FirstCategoryId":"1085","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acsfoodscitech.4c00918","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
This study explores the production of gelatin hydrolysates with metal-chelating peptides derived from red tilapia scales and investigates their biofunctional properties. Gelatin was enzymatically hydrolyzed using Alcalase (Alc-GH), Flavourzyme (Flav-GH), or a sequential combination of Alcalase and Flavourzyme (Alc+Flav-GH). Alc-GH and Alc+Flav-GH were ultrafiltrated at 1 kDa cutoff. Alc+Flav-GH, characterized by a high proportion of small-sized peptides, exhibited superior metal-chelating ability, as determined by switchSENSE and was associated with enhanced antioxidant activity. Ultrafiltration improved the Fe2+-chelating properties of both fractions compared to their respective whole hydrolysates. All of the hydrolysates and their ultrafiltrates showed remarkable ACE inhibitory activity. Specifically, the ≤1 kDa Alc-GH fraction produced small-sized Fe2+-chelating peptides with ACE inhibitory activity, whereas the ≤1 kDa Alc+Flav-GH fraction efficiently generated Ni2+-chelating peptides with strong antioxidant potential. LC-MS/MS data showed peptides rich in Asp, Glu, Ser, Lys, and Arg, which may contribute to their metal-chelating and antioxidant properties.