scispace - formally typeset
Journal ArticleDOI

Heat stability of forewarmed milks: influence of κ-casein, serum proteins and divalent cations

Patrick A. Morrissey, +1 more
- 01 Jun 1976 - 
- Vol. 43, Iss: 02, pp 267-274
TLDR
In this paper, the β-lg:κ-casein interaction was attributed mainly to a β-Lg-κ casein interaction, and it was concluded that milks which are destabilized by forewarming generally give a type A response (minimum in the pH-heat stability curves) and that preheat-stable milks generally gave a type B curve.
Abstract
Addition of isolated κ-casein to milk reduced the destabilizing influence of forewarming, while the addition of isolated β-lactoglobulin (β-lg) to the κ-casein-enriched systems resulted in a loss in stability on forewarming. This effect was ascribed mainly to a β-lg:κ-casein interaction. Some individual milks were unaffected by forewarming while others were markedly destabilized by the same treatment. Addition of Ca 2+ + Mg 2+ and interchanging of milk sera by dialysis influenced stability. It is concluded that milks which are destabilized by forewarming generally give a type A response (minimum in the pH–heat stability curves) and that preheat-stable milks generally give a type B curve (no minimum).

read more

Citations
More filters
Journal ArticleDOI

Heat-induced association of beta-lactoglobulin and casein micelles.

TL;DR: In this association, the formation of intermolecular S-S bonds between beta-lg and kappa-casein plays a role, but hydrophobic bonds are also involved, and no influence of alpha-la on the amount of associated beta- lg was found.
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

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.
Journal ArticleDOI

Physicochemical characterization of calcium-supplemented skim milk

TL;DR: In this paper, le calcul des equilibres ioniques dans les ultrafiltrats des different laits montre que les flux ioniques observes, controles principalement par les solubilites du phosphate and du citrate de calcium, ne modifient pas les produits d'activite ionique du phosphate dicalcique.
References
More filters
Journal ArticleDOI

Purification and Some of the Properties of αs-Casein and κ-Casein

TL;DR: In this paper, a starch-gel-urea electrophoresis was performed on α s -Casein and κ -casein and the results showed that α s-Casein was free of major contaminants, judged by starch-el urea-sodium chloride procedure with a final precipitation of impurities by ethanol.
Journal ArticleDOI

The stability of milk protein to heat: I. Subjective measurement of heat stability of milk

TL;DR: Coagulation time decreased by about 12% as rocking speed was increased over the range 4–12 c/min and increased by a factor of about 3 for a decrease in heating temperature of 10 degC over therange 140–105 °C; with some milks the Q 10 °C value increased to 5–8 a temperature decreased.
Journal ArticleDOI

The immune proteins of bovine colostrum and plasma.

TL;DR: In the present study, colostrum and the protein fractions derived from it have been studied electrophoretically and it was found that an electroph theoretically homogeneous globulin could be readily isolated in high yield by the conventional precipitation with ammonium sulfate.
Journal ArticleDOI

Influence of κ-casein and β-lactoglobulin on the Heat Stability of Skimmilk

TL;DR: In this paper, the authors classified individual cows according to their heat stability-pH relation as Type A (maximum and minimum heat stability) and Type B (no minimum heat stabilisation).
Journal ArticleDOI

Separation of β-Lactoglobulin from Other Milk Serum Proteins by Trichloroacetic Acid

TL;DR: In this article, a 3 × crystallized β-lactoglobulin was recovered with a specific rotation of −27.8 at 575 m μ, pH 4.75, intrinsic viscosity of 4.1, and an electrophoretic mobility of −5.65×10 −5 cm 2 /v/sec in veronal buffer pH 8.6, 0.1 ionic strength.
Related Papers (5)