Min You , Yanyan Chen , Chunhui Zhang , Feng Huang
{"title":"酸碱ph变化对牛肉肌肉肌原纤维蛋白结构和消化特性的影响","authors":"Min You , Yanyan Chen , Chunhui Zhang , Feng Huang","doi":"10.1016/j.foodchem.2025.146643","DOIUrl":null,"url":null,"abstract":"<div><div>The conformational changes and digestive properties of myofibrillar proteins (MPs) treated by various pH (pH 3, pH 7 and pH 12) or pH-shifting (pH 3 → 7 and pH 12 → 7) were investigated. The results showed that both acidic and alkaline treatments increased surface hydrophobicity. Acidic pH treatments enhanced protein aggregation and partially restored H<sub>0</sub> and the particle size of MPs. Under extreme pH conditions, α-helix of MPs may transform into β-sheets or random coil. The acidic and alkaline treatments significantly decreased the degree of hydrolysis compared to pH 7 (84.47 %, 49.45 %, and 69.03 %). Peptide composition indicated that acidic and alkaline treatments could influence the digestive sites of MPs by altering its head structure, while pH-shifting restores structural integrity, enabling pepsin and trypsin to access the same enzymatic hydrolysis sites. This study will provide insights into the structure and digestive properties of pH-shifting myofibrilar proteins, aiming to enhancing their nutritional formulation in meat processing.</div></div>","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"496 ","pages":"Article 146643"},"PeriodicalIF":9.8000,"publicationDate":"2025-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Effects of acidic and alkaline pH-shifting on structural and digestion characteristics of myofibrillar proteins of beef muscles\",\"authors\":\"Min You , Yanyan Chen , Chunhui Zhang , Feng Huang\",\"doi\":\"10.1016/j.foodchem.2025.146643\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The conformational changes and digestive properties of myofibrillar proteins (MPs) treated by various pH (pH 3, pH 7 and pH 12) or pH-shifting (pH 3 → 7 and pH 12 → 7) were investigated. The results showed that both acidic and alkaline treatments increased surface hydrophobicity. Acidic pH treatments enhanced protein aggregation and partially restored H<sub>0</sub> and the particle size of MPs. Under extreme pH conditions, α-helix of MPs may transform into β-sheets or random coil. The acidic and alkaline treatments significantly decreased the degree of hydrolysis compared to pH 7 (84.47 %, 49.45 %, and 69.03 %). Peptide composition indicated that acidic and alkaline treatments could influence the digestive sites of MPs by altering its head structure, while pH-shifting restores structural integrity, enabling pepsin and trypsin to access the same enzymatic hydrolysis sites. This study will provide insights into the structure and digestive properties of pH-shifting myofibrilar proteins, aiming to enhancing their nutritional formulation in meat processing.</div></div>\",\"PeriodicalId\":318,\"journal\":{\"name\":\"Food Chemistry\",\"volume\":\"496 \",\"pages\":\"Article 146643\"},\"PeriodicalIF\":9.8000,\"publicationDate\":\"2025-10-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0308814625038956\",\"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}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0308814625038956","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}
Effects of acidic and alkaline pH-shifting on structural and digestion characteristics of myofibrillar proteins of beef muscles
The conformational changes and digestive properties of myofibrillar proteins (MPs) treated by various pH (pH 3, pH 7 and pH 12) or pH-shifting (pH 3 → 7 and pH 12 → 7) were investigated. The results showed that both acidic and alkaline treatments increased surface hydrophobicity. Acidic pH treatments enhanced protein aggregation and partially restored H0 and the particle size of MPs. Under extreme pH conditions, α-helix of MPs may transform into β-sheets or random coil. The acidic and alkaline treatments significantly decreased the degree of hydrolysis compared to pH 7 (84.47 %, 49.45 %, and 69.03 %). Peptide composition indicated that acidic and alkaline treatments could influence the digestive sites of MPs by altering its head structure, while pH-shifting restores structural integrity, enabling pepsin and trypsin to access the same enzymatic hydrolysis sites. This study will provide insights into the structure and digestive properties of pH-shifting myofibrilar proteins, aiming to enhancing their nutritional formulation in meat processing.
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.