Keywords

Soy Peptide, Enzymatic Hydrolysis, Digestion, Molecular Weight, Polymerization, Ionic Strength

Abstract

Size exclusion chromatography and Folin-phenol method were used to determine the soybean peptides produced after enzymatic hydrolysis by acid proteases (Protease M, Pepsin), neutral proteases (Protease A, Protease N), and subtilis alkaline protease Alcalase. Simulate the changes in molecular weight after in vivo digestion and the effect of ionic strength on the polymerization of enzymatic hydrolyzate. The high performance liquid chromatography size exclusion chromatogram of soy peptides shows that about 50% of soy peptides have molecular weights concentrated between 10 and 30 kDa; after simulated intestinal pepsin and trypsin digestion, the molecular weight range of 3 to 30 kDa Peptide fragments vary relatively greatly. Folin-phenol method was used to determine the concentration of peptides in the enzymatic hydrolysis supernatant. The results showed that adding NaCl after enzymatic hydrolysis of gastric-peptide and A-peptide can significantly weaken the aggregation phenomenon, and adding NaCl before enzymatic hydrolysis of N-peptide can significantly weaken the aggregation phenomenon, regardless of where. Adding NaClM-peptide in any way will aggravate the polymerization phenomenon. The concentration of Alcalase-peptide is always maintained at about 11.40mg?mL-1, and the ionic strength has little effect on it.

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Original research done by Zhang Bin, Liu He, Xu Jingting, Guo Shuntang

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