Heat stability of milk: influence of modifying sulphydryl-disulphide interactions on the heat coagulation time–pH profile

Abstract

SummaryAddition of reducing agents such as 2-mercaptoethanol (2-ME), dithio-threitol and Na sulphite to milk markedly reduced its heat stability at pH values below 7·1. 2-ME reversibly destabilized milk or serum protein-free casein micelle dispersions and promoted the release of κ-casein-rich protein from the micelles. Reduction of either casein micelles or β-lactoglobulin (β-lg) with 2-ME and subsequent blocking of the newly formed –SH groups with N-ethylmaleimide irreversibly reduced the maximum to minimum ratio in the heat stability profile. 2-ME disrupted κ-casein/β-lg complexes and stripped κ-casein from the micelles on heating. The milk or caseinate systems were thus destabilized. Addition of KBrO4or iodosobenzoate to milk at 5 HIM eliminated the minimum but destabilized milk in the region of the maximum. However, KIO3at 5 mm had a strong stabilizing effect throughout the pH range 6·5–7·3.