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Journal ArticleDOI

Heat stability of milk: the mechanism of stabilization by formaldehyde

Harjinder Singh, +1 more
- 01 Feb 1985 - 
- Vol. 52, Iss: 1, pp 65-76
TLDR
In this article, it was shown that the minimum in the heat coagulation time (HCT)-pH curve was irreversibly removed if the milk was preheated at 80°C for 10 min in the presence of 5 mM-HCHO.
Abstract
The increase produced by formaldehyde (HCHO) in the heat stability of milk did not occur when milk was treated with HCHO at temperatures up to 60°C followed by dialysis at 5°C However, the minimum in the heat coagulation time (HCT)–pH curve was irreversibly removed if the milk was preheated at 80–C for 10 min in the presence of 5 mM-HCHO Although this treatment blocked the e-amino groups of lysyl residues, the stabilizing mechanism is considered to be due to the cross linking action of HCHO which reduced the level of non-sedimentable, κ-casein-rich protein dissociated from the micelles on heating The specific crosslinking agent, dimethyl suberimidate, modified the HCT-pH profile of milk in a manner similar to preheating at 80°C for 10 min with 5 mM-HCHO, supporting the crosslinking hypothesis The results of this study appear to lend some support to the proposal of Kudo (1980) that the minimum in the HCT-pH curve of milk is due to the dissociation of κ-casein from the micelles on heating at high temperatures at pH values greater than 6η7

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Citations
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Book ChapterDOI

Structure and stability of bovine casein micelles.

TL;DR: The appearance, substructure, size distribution, voluminosity, and dissociation of casein micelles are discussed in the chapter and the forces involved in coagulation, steric stabilization of mouselles, and action of chymosin are emphasized.
Journal ArticleDOI

Heat stability of milk

TL;DR: In this article, the authors provide an overview of the factors that influence the pH dependence of the heat stability of normal and concentrated milks and discuss the principal heat-induced changes in the milk system that contribute to coagulation.
Book ChapterDOI

Heat-Induced Coagulation of Milk

TL;DR: In this paper, the effects of compositional factors, processing conditions and additives on the heat stability of milk are reviewed and the changes that occur on heating are considered in relation to heat stability.
Journal ArticleDOI

Modification of food proteins by covalent crosslinking

TL;DR: In this article, a review examines the naturally occurring covalent crosslinks present in proteins, the crosslinking of proteins that occurs during food processing, the various techniques used to introduce new crosslinks into proteins, and the possibilities of using such techniques to modify the functional properties of food proteins.
Journal ArticleDOI

Heat stability of milk: pH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures

TL;DR: In this article, the casein micelles were unstable after heating at pH 6·6, 6·8, 7·0 or 7·2, without significantly affecting the maximum stability.
References
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Journal ArticleDOI

The thiobarbituric acid assay of sialic acids.

TL;DR: This chapter discusses the different aspects of thiobarbituric acid assay of sialic acid, which is suitable for measuring the release of bound sialoic acid by sialidase and hydrolysis of sIALic acid-containing material must be carried out for the measurement of total sialsic acids.
Journal ArticleDOI

Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins

TL;DR: Application of the disc electrophoresis method to two proteins composed of dissimilar protomers, native aspartate transcarbamylase and tryptophan synthetase alpha(2)beta(2), revealed differences in the reactivities of the different kinds of protomer within each oligomer.
Book ChapterDOI

The Reactions of Formaldehyde with Amino Acids and Proteins

TL;DR: This chapter focuses on the reactions of formaldehyde with amino acid and proteins, a reagent familiar to all protein chemists through its employment in the formol titration of amino acids and peptides.