Identification of potential inhibitory peptides of enzymes involved in the metabolic syndrome obtained by simulated gastrointestinal digestion of fermented bean (Phaseolus vulgaris L.) seeds

- Proteins of bean fermented seeds are a source metabolic syndrome inhibitory peptide
- Fermentation improves inhibitory activity of peptides from bean proteins
- Optimum fermentation conditions depend on specific activity of peptides
- The sequences of peptide derived from bean proteins were determined

The aim of this study was to determine the conditions of bean fermentation carried out by Lactobacillus plantarum to obtain biologically active peptide fractions after in vitro digestion.The results suggest that optimum process conditions should be selected according to the specific activity of peptides. Only a fraction with a molecular mass of 3.5-7 kDa obtained after fermentation at 22 °C for 3 h had α-amylase inhibitory activity. The optimal fermentation conditions for bean seeds to release peptide fractions with a molecular mass of 3.5-7.0 kDa and the highest lipase or ACE inhibitory activity (IC50 1.19 and 0.28 mg mL− 1, respectively) were determined as 30 °C and 3 days. The fractions with the highest inhibitory activity were identified by LC-MS/MS and the sequences of the peptide derived from bean proteins were determined as INEGSLLLPH, FVVAEQAGNEEGFE, SGGGGGGVAGAATASR, GSGGGGGGGFGGPRR, INEGSLLLPH, GGYQGGGYGGNSGGGYGNRG, GGSGGGGGSSSGRRP, and GDTVTVEFDTFLSR.

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