To increase the value-added utilization of cottonseed protein,xanthine oxidase(XOD)inhibitory peptides were prepared via enzymatic hydrolysis,and the XOD-inhibitory potency and degree of hydrolysis(DH)were used as eva...To increase the value-added utilization of cottonseed protein,xanthine oxidase(XOD)inhibitory peptides were prepared via enzymatic hydrolysis,and the XOD-inhibitory potency and degree of hydrolysis(DH)were used as evaluation metrics.The optimal hydrolysis with alkaline protease was pinpointed by combining single-factor screens with response-surface refinement;at pH 9,50℃,1:10(g/mL)solid-to-liquid load and 10000 U/g enzyme,a 3 h reaction delivered hydrolysates exhibiting 96.61%±0.58%XOD inhibition and 44.29%±0.35%DH.Amino acid composition and molecular weight analyses indicated that the peptides were rich in hydro-phobic residues and predominantly low in molecular weight.Fourier transform infrared spectroscopy(FTIR)showed a secondary structure dominated byβ-turns.Following simulated gastrointestinal digestion,the hy-drolysates retained 72.02%of their XOD inhibitory activity.These findings provide a preliminary character-ization of the XOD inhibitory activity,molecular size distribution,and secondary structural features of cottonseed peptides obtained under optimized hydrolytic conditions.This information may serve as a reference for future peptide optimization and further in vivo and safety studies.展开更多
基金funded by XPCC Guiding Science and Technology Program of China(grant number 2024DZ006)Research Project of Xinjiang Academy of Agricultural and Reclamation Science in China(grant number 2024YJPY04).
文摘To increase the value-added utilization of cottonseed protein,xanthine oxidase(XOD)inhibitory peptides were prepared via enzymatic hydrolysis,and the XOD-inhibitory potency and degree of hydrolysis(DH)were used as evaluation metrics.The optimal hydrolysis with alkaline protease was pinpointed by combining single-factor screens with response-surface refinement;at pH 9,50℃,1:10(g/mL)solid-to-liquid load and 10000 U/g enzyme,a 3 h reaction delivered hydrolysates exhibiting 96.61%±0.58%XOD inhibition and 44.29%±0.35%DH.Amino acid composition and molecular weight analyses indicated that the peptides were rich in hydro-phobic residues and predominantly low in molecular weight.Fourier transform infrared spectroscopy(FTIR)showed a secondary structure dominated byβ-turns.Following simulated gastrointestinal digestion,the hy-drolysates retained 72.02%of their XOD inhibitory activity.These findings provide a preliminary character-ization of the XOD inhibitory activity,molecular size distribution,and secondary structural features of cottonseed peptides obtained under optimized hydrolytic conditions.This information may serve as a reference for future peptide optimization and further in vivo and safety studies.
