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

• Published in: Food science & technology Vol. 29; no. 8; pp. 763 - 766
• Main Authors: Shimoyamada, M., Yoshimura, H., Tomida, K., Watanabe, K.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.01.1996; Elsevier
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; beta-lactoglobulin; binding proteins; Biological and medical sciences; Food industries; Fundamental and applied biological sciences. Psychology; heat stability; retinoic acid; stabilizing; vitamin A; Serine endopeptidases; Enzyme; Free form; Retinoids; Thermal stability; Retinol; Resistance; Peptidases; Trypsin; Ultraviolet irradiation; Proteolysis; Hydrolases; Molecular complex; Oxidation; Whey protein; Retinoic acid; Comparative study
• ISSN: 0023-6438; 1096-1127
• DOI: 10.1006/fstl.1996.0119

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.