| Abstract
| - The effects of ascorbic acid on the riboflavin-sensitized photochemical changes in β-lactoglobulin inan aqueous buffer solution as determined by high performance gel permeation liquid chromatography(HPGPLC), insoluble protein content, and individual amino acid content during fluorescent lightillumination were studied. The riboflavin-sensitized photochemical degradation of β-lactoglobulinwas effectively inhibited by ascorbic acid, and its inhibitory effectiveness was concentrationdependent. The 0.1% ascorbic acid treatment showed 74.4% inhibition of β-lactoglobulin degradationas determined by a HPGPLC during 6 h light illumination. Insolubility of β-lactoglobulin in a buffersolution during light illumination was also effectively decreased by ascorbic acid treatment. Theriboflavin-sensitized photochemical reduction of cysteine, histidine, lysine, methionine, and tryptophan in β-lactoglobulin was high during 6 h fluorescent light illumination. The 0.1% ascorbicacid treatment exhibited 20.8% inhibition of total amino acid degradation in β-lactoglobulin during6 h light illumination, showing strong inhibitory activity against the degradation of arginine, asparticacid, cystein, glycine, histidine, phenylalanine, proline, serine, and tryptophan. Keywords: β-lactoglobulin; riboflavin; ascorbic acid; insoluble protein; amino acids
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