Abstract:To obtain high-purity phycocyanin hydrolysate peptides with uric acid-lowering function,phycocyanin was used as the raw material,and alkaline protease was selected as the optimal hydrolase,followed by evaluation of the activity of the enzymatic hydrolysates.The phycocyanin uric acid-lowering peptides were separated,purified and identified by ultrafiltration,gel filtration chromatography,and reverse-phase high performance liquid chromatography.Meanwhile,the uric acid-lowering activity was verified by the xanthine oxidase（XO） inhibition test.The results showed that the fraction with a molecular weight less than 3 kDa of the phycocyanin enzymatic hydrolysates after separation and purification exhibited the strongest XO inhibition activity.Further purification identified two active peptide sequences：the pentapeptide CPGVC （molecular weight 477.17 Da） and the octapeptide FPTLVRPT （molecular weight 929.53 Da）.Chemical synthesis verification indicated that the active peptide segments CPGVC and FPTLVRPT,identified from phycocyanin,both had good XO inhibition activity.Moreover,the single peptide segment CPGVC and its complex demonstrated significant XO inhibition ability,among which CPGVC possessed the strongest activity.