Author:
Chobert Jean-Marc,Touati Abdelmadjid,Bertrand-Harb Catherine,Dalgalarrondo Michele,Nicolas Marie-Georgette,Haertle Tomasz
Abstract
Summaryβ-Casein amino groups were modified with aldehydes and dialdehydes via reductive alkylation at pH 8·0. The degree of alkylation was controlled by the amount of the alkylating reagent applied. The initial rates of α-chymotrypsin-catalysed hydrolysis of alkylated β-casein were inversely related to the size of the modifying group. Proteolysis of modified β-casein with trypsin (18 h) or with α-chymotrypsin (48 h) depended on the nature and size of the substituent applied. The measurements of tryptophan fluorescence indicate that the modifications also induced conformation change. Solubilities of methyl-, ethyl- or benzyl-β-casein slightly increased; solubilities of β-casein dialdehyde derivatives were significantly lower than that of native β-casein. Emulsion stability of methyl- or ethyl- β-casein was higher than that of native β-casein in the acidic pH range. After modification with glyoxal, the emulsifying activity and the emulsion stability of β-casein decreased. The emulsifying activity of benzyl- β-casein was lower than that of native β-casein. Phthalylated β-casein displayed the poorest emulsion stability.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
Cited by
18 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献