Abstract
ABSTRACT: Films were formed from heated whey protein isolate (WPI) solutions (heated [H] films) and from unheated WPI solutions following adjustment to pH 11, with subsequent readjustment to pH 7 (unheated, readjusted [UR] films) or without readjustment to pH 7 (unheated, unadjusted films [UU] films). UU and UR films had significantly lower % elongation, tensile strength, and Young's modulus than H films. Film solubility and dispersion in water were in the order: H films < UU films < UR films. Free sulphydryl groups were lower and disulphide‐mediated polymerization was higher in heated than in unheated WPI solutions whereas solubility of H films increased in the presence of dithiothreitol.
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