Study on antioxidant peptide activity and functional properties of Rumex leaf protein

This article aimed to explore the antioxidant properties of Rumex leaf protein hydrolyzate and Rumex leaf protein functional properties,which could provide a theoretical basis for Rumex leaf protein application and promotion.In this study,the leaf proteins obtained by alkaline heat treatment were hydrolyzed by trypsin and pepsin separately,and the hydrolysates ability of free radical scavenging and chelated metal ions were evaluated. In addition,the study also discussed the effect of different temperature,p H,Na Cl concentration on Rumex leaf protein solubility,water binding capacity,oil binding capacity,foaming and emulsifying properties.The results showed that,when the peptide concentrations were 0.5,1,8,and 0.2 mg / m L separately,the reducing power,the scavenging ability of DPPH,·OH and Fe2 +chelating ability of tryptic peptides were significantly higher than pepsin peptides( p < 0.05). When the peptide concentration was 80 mg / m L,pepsin peptides on the scavenging O-2·significantly was higher than the tryptic peptides. The differences in the types and effects of free radical scavenging of the two peptides might be related to the type and quantity of hydrophobic amino acids in the peptides derived from the enzymatic hydrolysis.Functional properties of leaf protein showed that Rumex leaf protein was of high water binding capacity( > 4 g / g) and foaminess( up to a maximum of 45%),which were less affected by temperature,p H and Na Cl concentration. However,the solubility,oil bingding capacity and emulsifying affected by temperature,p H and Na Cl concentration showed the regular difference and fluctuation a certain range.