Liangting Shao, Junming Gong, Yang Dong, Silu Liu, Xinglian Xu, Huhu Wang
{"title":"Hydrolyzing collagen by extracellular protease hap of Aeromonas salmonicida: Turning chicken by-products into bioactive resources","authors":"Liangting Shao, Junming Gong, Yang Dong, Silu Liu, Xinglian Xu, Huhu Wang","doi":"10.1016/j.foodchem.2025.142778","DOIUrl":null,"url":null,"abstract":"Collagen-rich meat processing by-products have potential utilization value. Extracellular protease Hap from meat-borne <em>Aeromonas salmonicida</em> has been identified as an ideal protease for hydrolyzing collagen. Here, to explore the possible application of Hap for giving chicken by-products a high added value, the hydrolysis ability and mechanism were investigated. With a V<sub>max</sub> of 31.9 μg/mL/min and a K<sub>m</sub> of 1.18 mg/mL, Hap demonstrated obvious substrate specificity to pepsin-solubilized collagen (PSC) derived from chicken by-products, and significantly affected the tertiary structure and microstructure of PSC. Hap was found to preferentially cleave the peptide bond between Gly-X by peptide release kinetics, attacking from two ends to the middle region for α1 chain. Sixteen peptides are anticipated to be non-toxic with twenty potential biological activities at the end of hydrolysis. These observations will enrich the collagen hydrolysis mechanism of protease secreted by meat-borne bacteria and provide new insights into the utilization of meat by-products.","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"99 1","pages":""},"PeriodicalIF":8.5000,"publicationDate":"2025-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1016/j.foodchem.2025.142778","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
Collagen-rich meat processing by-products have potential utilization value. Extracellular protease Hap from meat-borne Aeromonas salmonicida has been identified as an ideal protease for hydrolyzing collagen. Here, to explore the possible application of Hap for giving chicken by-products a high added value, the hydrolysis ability and mechanism were investigated. With a Vmax of 31.9 μg/mL/min and a Km of 1.18 mg/mL, Hap demonstrated obvious substrate specificity to pepsin-solubilized collagen (PSC) derived from chicken by-products, and significantly affected the tertiary structure and microstructure of PSC. Hap was found to preferentially cleave the peptide bond between Gly-X by peptide release kinetics, attacking from two ends to the middle region for α1 chain. Sixteen peptides are anticipated to be non-toxic with twenty potential biological activities at the end of hydrolysis. These observations will enrich the collagen hydrolysis mechanism of protease secreted by meat-borne bacteria and provide new insights into the utilization of meat by-products.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.