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Int J Biol Macromol ; 56: 41-8, 2013 May.
Article in English | MEDLINE | ID: mdl-23384487

ABSTRACT

Although heat treatment of proteins is believed to promote and accelerate glycation, the accompanying structural changes in proteins because of heat denaturation and/or glycation are not completely understood. In addition, there is an increasing interest for inhibitors of thermal glycation in food processing. ß-Carotene is a naturally occurring carotenoid found in many vegetables, fruits and herbs, with known antioxidant activity. However, it has not been identified if ß-carotene possesses anti-glycation activity. We have tested the anti-glycation capacity of ß-carotene in the bovine serum albumin (BSA)/glucose system that was heated to 55 and 65 °C for 3 days and studied the level of glycation, conformational alterations in BSA, and changes in hydrophobicity, due to thermal treatment and/or glycation. ß-Carotene exhibited significant inhibitory effects on the formation of advanced glycation end products (AGEs) and also prevented the secondary structural changes in BSA due to thermal glycation. Our results represent the anti-glycative properties of ß-carotene in food systems where such thermal conditions prevail.


Subject(s)
Serum Albumin, Bovine/metabolism , Temperature , beta Carotene/metabolism , Animals , Cattle , Circular Dichroism , Glucose/metabolism , Glycation End Products, Advanced/metabolism , Glycosylation , Hydrophobic and Hydrophilic Interactions , Maillard Reaction , Protein Carbonylation , Protein Structure, Secondary , Serum Albumin, Bovine/chemistry , Spectrometry, Fluorescence , Tryptophan/metabolism
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