{"title":"Effect of dephosphorylation on calcium binding to αs1-casein-enriched protein","authors":"","doi":"10.1016/j.idairyj.2024.106030","DOIUrl":null,"url":null,"abstract":"<div><p>The calcium binding to enriched α<sub>s1</sub>-casein (71 % α<sub>s1</sub>-casein on a protein basis) that was native or dephosphorylated to different extents was studied using a calcium ion selective electrode and at an ionic strength comparable to that found in milk. The calcium binding to α<sub>s1</sub>-casein decreased as the level of dephosphorylation was increased. Langmuir adsorption modelling of the calcium binding gave the maximum calcium binding and calcium binding affinity for the native α<sub>s1</sub>-casein and progressively dephosphorylated α<sub>s1</sub>-casein. This evaluation indicated that the number of calcium binding sites on α<sub>s1</sub>-casein decreased as dephosphorylation increased; however, the affinity for any remaining calcium binding sites was unchanged. Correlations were observed between calcium binding of native and dephosphorylated α<sub>s1</sub>-casein with the calculated charge at pH 7.0, or the calculated or experimentally determined isoelectric pH of the α<sub>s1</sub>-casein. Understanding the calcium binding to native and dephosphorylated α<sub>s1</sub>-casein is important in understanding casein association in systems such as natural and artificial casein micelles.</p></div>","PeriodicalId":13854,"journal":{"name":"International Dairy Journal","volume":null,"pages":null},"PeriodicalIF":3.1000,"publicationDate":"2024-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Dairy Journal","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S095869462400150X","RegionNum":3,"RegionCategory":"农林科学","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
The calcium binding to enriched αs1-casein (71 % αs1-casein on a protein basis) that was native or dephosphorylated to different extents was studied using a calcium ion selective electrode and at an ionic strength comparable to that found in milk. The calcium binding to αs1-casein decreased as the level of dephosphorylation was increased. Langmuir adsorption modelling of the calcium binding gave the maximum calcium binding and calcium binding affinity for the native αs1-casein and progressively dephosphorylated αs1-casein. This evaluation indicated that the number of calcium binding sites on αs1-casein decreased as dephosphorylation increased; however, the affinity for any remaining calcium binding sites was unchanged. Correlations were observed between calcium binding of native and dephosphorylated αs1-casein with the calculated charge at pH 7.0, or the calculated or experimentally determined isoelectric pH of the αs1-casein. Understanding the calcium binding to native and dephosphorylated αs1-casein is important in understanding casein association in systems such as natural and artificial casein micelles.
期刊介绍:
The International Dairy Journal publishes significant advancements in dairy science and technology in the form of research articles and critical reviews that are of relevance to the broader international dairy community. Within this scope, research on the science and technology of milk and dairy products and the nutritional and health aspects of dairy foods are included; the journal pays particular attention to applied research and its interface with the dairy industry.
The journal''s coverage includes the following, where directly applicable to dairy science and technology:
• Chemistry and physico-chemical properties of milk constituents
• Microbiology, food safety, enzymology, biotechnology
• Processing and engineering
• Emulsion science, food structure, and texture
• Raw material quality and effect on relevant products
• Flavour and off-flavour development
• Technological functionality and applications of dairy ingredients
• Sensory and consumer sciences
• Nutrition and substantiation of human health implications of milk components or dairy products
International Dairy Journal does not publish papers related to milk production, animal health and other aspects of on-farm milk production unless there is a clear relationship to dairy technology, human health or final product quality.