Action of Heat on Cow κ-Casein. Heat Caseino-Glycopeptide
Open Access
- 1 November 1967
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 50 (11) , 1738-1743
- https://doi.org/10.3168/jds.s0022-0302(67)87709-9
Abstract
The 3 main casein fractions ([alpha]5, [beta], [kappa]) of cow milk were attacked during heating, under conditions closely related to sterilization, but the process was probably different in each case. For n-casein, the actions of rennin and of heat (120 C- 20 min.) seem to be similar. A heat caseino-glycopeptide was isolated and it had nearly the same amino acid composition as the rennin caseino-glycopeptide. These data again suggest the existence of a very labile linkage in k-casein which is easily split by different procedures.This publication has 10 references indexed in Scilit:
- Isolation, Purification, and Analysis of Two κ-Casein-like Fractions from Sheep CaseinJournal of Dairy Science, 1967
- Genetic Polymorphism in Caseins of Cow's Milk. III. Isolation and Properties of αs1-Caseins A, B, and CJournal of Dairy Science, 1964
- Preparation of β-casein by a modified urea fractionation methodJournal of Dairy Research, 1963
- Étude de la Caséine κ de vache caractérisation de la liaison sensible à l'action de la présureBiochimica et Biophysica Acta, 1963
- Dephosphorization of Casein by Heat Treatment. I. In Caseinate SolutionsJournal of Dairy Science, 1962
- Étude comparée des caséino-glycopeptides formés par action de la présure sur les caséines de vache, de brebis et de chèvreBiochimica et Biophysica Acta, 1961
- An improved method for the isolation of κ-caseinBiochimica et Biophysica Acta, 1961
- The Effect of Processing on the Nitrogen Distribution in MilkJournal of Dairy Science, 1941
- 146. The heat denaturation of albumin and globulin in milk. II. Denaturation and degradation of protein at temperatures of 75–120° CJournal of Dairy Research, 1937
- The heat-coagulation of caseinogenBiochemical Journal, 1934