Translated Title
Study on preparation, structure and activity of soybean protein isolate peptide-se complex
Translated Abstract
Soybean protein isolate peptides (SPIP) were prepared by the biological enzymolysis technology, and the enzymolysis technology was optimized by response surface methodology using selenium binding capacity as an indicator.Results showed that optimized enzymatic hydrolysis condition was: temperature 50℃, enzyme-substrate ratio 5% (w/w), substrate concentration 3%, with a hydrolysis degree of 23.57%.To optimize the chelation technology of soybean protein isolate peptide-Se complex (SPIP-Se), the response surface method was used.Results showed that optimized chelation technology condition was : reaction time 2h, reaction temperature 78℃, pH10, the maximum selenium binding capacity of SPIP was 46.143 mg/g.And the structure properties of SPIP-Se were characterized by absorption spectrum and fluorescence spectrum.The results indicated that the principal sites of selenium-binding corresponded to the carboxyl groups and carbonyl groups of SPIP.In addition, the research on hydroxyl radical scavenging activity, reducing power, metal chelating capacity and lipid peroxidation inhibition acticity showed that SPIP-Se had antioxidative effects in vitro to different degrees.
Translated Keyword
antioxidant
bioactive peptides
chelation
Se
soybean protein isolate
