Bovine Beta Lactoglobulin A Investigated for Structural Changes Induced by Mechanical Agitation, pH and Heat

Abstract

　The effect of agitation, pH and heat on the structural of bovine β-lactoglobulin A was investigated by circular dichroism and spectrophotometry. The α-helices, β-turns, β-sheets and random coils of β-lactoglobulin A were severely altered by the application of heat at various pH levels. Considerably vigorous agitation of β-lactoglobulin A significantly changed the secondary structure. The SH content of β-lactoglobulin A was higher in acid pH and it sharply decreased at alkaline pH. Secondary structure of β-lactoglobulin A was collapsed on heating of the solutions that had pH 12 or higher.