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Stabilities of Bovine β-Lactoglobulin/Retinol or Retinoic Acid Complexes Against Tryptic Hydrolysis, Heating and Light-induced Oxidation

Authors
Journal
LWT - Food Science and Technology
0023-6438
Publisher
Elsevier
Publication Date
Volume
29
Issue
8
Identifiers
DOI: 10.1006/fstl.1996.0119

Abstract

Abstract Complexes of β-lactoglobulin and retinol or retinoic acid were subjected to tryptic hydrolysis. Susceptibilities of β-lactoglobulin/retinol and β-lactoglobulin/retinoic acid complexes to tryptic hydrolysis were significantly lower than that of free β-lactoglobulin. The Stokes radii of β-lactoglobulin/retinol (2·2 nm) and β-lactoglobulin/retinoic acid (2·3 nm) estimated by gel filtration chromatography were relatively smaller than that of β-lactoglobulin (2·57 nm). Heat stabilities of β-lactoglobulin/retinol and β-lactoglobulin/retinoic acid complexes increased significantly on heating at 60 °C for 10 min. β-Lactoglobulin/retinoic acid complex was more heat stable than β-lactoglobulin/retinol. Retinol and retinoic acid bound to βlactoglobulin were less susceptible to light-induced oxidation by UV-light irradiation than those which were free or bound to bovine serum albumin.

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