Riboflavin-sensitized photochemical changes in β-lactoglobulin in an aqueous buffer solution as affected by ascorbic acid

The effects of ascorbic acid on the riboflavin-sensitized photochemical changes in beta-lactoglobulin in an aqueous buffer solution as determined by high performance gel permeation liquid chromatography (HPGPLC), insoluble protein content, and individual amino acid content during fluorescent light illumination were studied. The riboflavin-sensitized photochemical degradation of beta-lactoglobulin was effectively inhibited by ascorbic acid, and its inhibitory effectiveness wa's concentration dependent. The 0.1% ascorbic acid treatment showed 74.4% inhibition of beta-lactoglobulin degradation as determined by a HPGPLC during 6 h light illumination. Insolubility of beta-lactoglobulin in a buffer solution during light illumination was also effectively decreased by ascorbic acid treatment. The riboflavin-sensitized photochemical reduction of cysteine, histidine, lysine, methionine, and tryptophan in beta-lactoglobulin was high during 6 h fluorescent light illumination. The 0.1% ascorbic acid treatment exhibited 20.8% inhibition of total amino acid degradation in beta-lactoglobulin during 6 h light illumination, showing strong inhibitory activity against the degradation of arginine, aspartic acid, cystein, glycine, histidine, phenylalanine, proline, serine, and tryptophan.