Abstract
This study aimed to investigate the dipeptide amino acid profiles correlated with xanthine oxidase (XOD) inhibitory activity and guide screening to determine suitable sources for XOD inhibitor protein hydrolysate preparation. The XOD inhibitory activities of 400 dipeptides were predicted via molecular docking and measured in vitro, and amino acids containing aromatic structures and charged residues were correlated with high XOD inhibitory properties. Subsequently, the effects of Cys-Glu and Lys-Glu, which showed the highest in vitro activities, were examined in hyperuricaemic mice, and were found to alleviate hyperuricaemia and modulate the gut microbiota. Furthermore, a suitable protein from Oreochromis mossambicus with high contents of charged (8.6%) and aromatic (1.67%) amino acids was screened, and the in vitro inhibitory rates of protein hydrolysate prepared from O. mossambicus against XOD were found to be 21.90% and 44.51% at 40 and 100 mg/ml, respectively. This study provides a strategy for screening protein hydrolysate sources with certain activities based on amino acid profiles.
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