Abstract
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•V.faba hydrolysate showed antioxidant, antityrosinase and antibiofilm activities.•Seven peptides P1-P7 were isolated, identified and chemically synthesized.•Peptide P6 was the most effective to quench DPPH. and inhibit tyrosinase activity.•Peptide P5 was the only peptide able to chelate iron and reduce Fe3+.•Peptide P7 showed the highest antibiofilm activity against P. aeruginosa PA14.
The aim of this study was to identify peptides with antioxidant, antityrosinase and antibiofilm activities released from Vicia faba seed proteins hydrolysate. The hydrolysis pattern was performed with trypsin. Firstly, the obtained hydrolysate was fractionated by cation exchange chromatography and the fraction exhibiting the highest biological activity was then analyzed by reverse phase HPLC tandem mass spectrometry. After annotation by Peaks software (BSI, Canada) for de novo peptide sequencing, seven peptides were identified, mainly derived from storage proteins: legumin and vicilin. These peptides were further chemically synthesized to assess their antioxidant capacity, antityrosinase activity and antibiofilm ability against Pseudomonas aeruginosa PA14. Results showed that peptides P5, P6 and P7 identified as LSPGDVLVIPAGYPVAIK, VESEAGLTETWNPNHPELR and EEYDEEKEQGEEEIR respectively, displayed the highest DPPH radical scavenging activity (IC50=0.25–1.9mM). P5 was the only peptide able to chelate iron and reduce Fe3+ to Fe2+. Furthermore, peptides P4 (GPLVHPQSQSQSN) and P6 were observed as potent tyrosinase inhibitors with IC50 values of 1 and 0.14mM respectively. P1, P5, P6 and P7 also showed interesting antibiofilm activity against Pseudomonas aeruginosa PA14 with MBIC50 value ranged from 12 to 35μM. Our data suggest that V. faba seed proteins hydrolysate could be potentially used as a source of natural bioactive peptides for cosmetic and pharmaceutical applications.