Study on the physical and chemical properties of rice residue peptide

Rice residue protein was hydrolyzed by alkaline protease to produce angiotensin-converting enzyme inhibitory peptide in this passage. The properties of peptide such as solubility,emulsifying and emulsion stability,foaming and foaming stability in different pH conditions were studied. And the function of promoting yeast fermentation activity and amino acid composition were also studied. The results showed that:rice residue peptide had good solubility and not precipitated in the isoelectric point. It can be used as a nitrogen material to promote microbial fermentation. After rice protein residue was hydrolysated by enzyme,the hydrophobic amino acids and lysine increased 10 times than rice residue protein,and greatly improved the ratio of amino acid patterns.