Abstract: Highland barley fermentation spent (HBFS) is a wine spent from pure grain, which is rich in nutrients, including high quality proteins, and can be used to prepare peptides. To further investigate the functional activity of HBFS peptides, HBFS proteins were extracted by alcohol-base, alkali and acid methods, purified using a protein purifier, and the purified proteins were analyzed qualitatively and quantitatively, and sobriety and in vitro antioxidant activity experiments were carried out. The results showed that the yield of protein extraction by the alcohol-base method was higher than that of the other two methods, with a yield of (7.52±0.12)%. Twenty-nine proteins were identified in the qualitative and quantitative analysis, and eleven proteins were differentially expressed by the alcohol-base method compared with the alkaline method. The differential proteins were mainly related to microbial metabolism, oxidative phosphorylation and biosynthesis of secondary metabolites. In addition, the optimal effect on ADH activation was (22.58±0.53)% at a peptide concentration of 10 mg/mL. And when the peptide concentration was 21 μg/L, the scavenging effects on DPPH radical, ·OH and ·O-2 were (70.76±1.35)%, (52.05±2.09)% and (55.88±1.99)%, respectively. The results validate the possibility of functional active peptide extraction in HBFS and also provide a reference for subsequent studies on the functionality of HBFS peptides.
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