Preparation, Amino Acid Composition and Activity of Tartary Buckwheat Protein Lipid-lowering Peptide

Abstract

Tartary buckwheat was used as raw material to extract tartary buckwheat protein, and the enzymatic hydrolysis conditions of tartary buckwheat protein lipid-lowering peptides were screened by single factor and response surface optimization experiments using the inhibition rate of pancreatic lipase as index. The amino acid composition and lipid lowering activity of lipid-lowering peptides were studied. The results showed that the lipid-lowering peptides obtained from tartary buckwheat protein with bromelain had higher inhibitory activity on pancreatic lipase. The optimal enzymatic hydrolysis conditions were hydrolysis time 2.1 h, hydrolysis temperature 62.0 ℃, substrate concentration 3.23%, pH7.0 and enzyme substrate ratio 0.4%. Under these conditions, the inhibitory rate of pancreatic lipase was 81.22%±0.16%. Amino acid analysis showed that essential amino acids, hydrophobic amino acids and acidic amino acids accounted for 27.82%, 32.11%, 35.86%, and the ratio of arginine to lysine was 2.28. The EC50/IC50 values of sodium taurine cholic acid binding rate, cholesterol esterase inhibition rate and pancreatic lipase inhibition rate were 9.136, 3.902 and 0.051 mg/mL, respectively. The results provided a new idea and theoretical basis for the high-value utilization of tartary buckwheat resources and the development of tartary buckwheat protein active peptides.

Keywords

• tartary buckwheat protein
• enzymatic hydrolysis
• response surface optimization
• lipid-lowering peptides
• amino acid composition
• evaluation of activity