Improving the antioxidant and antidiabetic properties of common bean proteins by enzymatic hydrolysis using a blend of proteases

Bioactive peptides are fragments of polypeptide chains with specific sequence of amino acids that can promote positive effects on human health. A potential substrate to obtaining these compounds is the common bean (Phaseolus vulgaris L. cv Carioca) due to its high protein content. In this sense, the objective of this study was to evaluate the antioxidant and antidiabetic properties of common bean protein hydrolysates. The proteases Flavourzyme™ 500L, Alcalase™ 2.4 L and Neutrase™ 0.8 L were applied individually and in binary/ternary combinations, using a statistical mixture design. The antioxidant properties were evaluated by the DPPH radical-scavenging activity, total antioxidant capacity and iron reduction power. The inhibition of the enzymes α-amylase and α-glucosidase was used to assess the antidiabetic properties of the protein hydrolysates. The modification of common bean proteins resulted in hydrolysates with antioxidant activities up to 32% higher than non-hydrolyzed samples. Also, the antidiabetic potential was evidenced by the total inhibition of α-amylase activity and inhibition of α-glucosidase in approximately 35%. Our results demonstrated that protein fractions of common bean produced by multiple hydrolysis can be an alternative strategy to produce bioactive peptides using a natural, popular and inexpensive protein source.