Physical Changes in Milk Proteins at Elevated Temperatures as Determined by Light Scattering. II. Interaction between β-Lactoglobulin and Whole, α-, and κ-Casein in Buffer
Open Access
- 1 February 1964
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 47 (2) , 126-131
- https://doi.org/10.3168/jds.s0022-0302(64)88604-5
Abstract
Application of the technic of light scattering to the study of heat induced bovine milk casein interactions with [beta]-lactoglobulin was made. Marked aggregation of [beta] -lactoglobulin was observed at 70 and 90 C. Interaction of both [alpha]-casein and K-casein with [beta]-lactoglobulin was observed at 90 C, but not with [alpha]-casein at 30 C. The addition of para-hydroxymer-curibenzoate inhibited the stabilizing interaction at elevated temperatures. Covering the air surface of [beta]-lactoglobulin solutions and [beta]-lactoglobulin-casein mixtures with mineral oil prevented the appearance of a precipitate at the surface.This publication has 2 references indexed in Scilit:
- Physical Changes in Milk Proteins at Elevated Temperatures as Determined by Light Scattering. I. Casein FractionsJournal of Dairy Science, 1964
- Heat Denaturation of β-Lactoglobulins A and BJournal of Dairy Science, 1962