CARIOCA BEAN (PHASEOLUS VULGARIS CV. CARIOCA) PROTEIN HYDROLYSATES AS POTENTIAL SOURCES OF PEPTIDES WITH ANTI-DIABETIC ACTIVITY: IN VITRO INHIBITION OF α-AMYLASE AND α-GLUCOSIDASE
Common bean is a legume rich in protein and has been attracting the interest of research globally by the presence of specific protein fragments that have a positive impact on human health and food systems. These compounds are defined as biologically active peptides and can be released from the parent protein by enzymatic hydrolysis. In this study, hydrolysates from Carioca bean protein concentrate were produced using three different proteolytic enzymes and their binary or ternary mixtures. The protein hydrolysates were evaluated as potential sources of peptides with anti-diabetic activity by the inhibition of enzymatic activity of α-amylase and α-glucosidase. The samples were evaluated at 1 mg/mL. The results showed that the enzymatic hydrolysis using different protease combinations resulted in synergistic effects, increasing the anti-diabetic properties of the Carioca bean protein. Compared to the parent protein, % α-amylase inhibition increased from 4.7% (non-hydrolyzed protein) to 100% for the hydrolysates obtained using the combination of the proteases Neutrase 0.8L and Alcalase 2.4L, in equal proportions. The protein hydrolysates obtained with the enzymes applied individually also had high anti-diabetic potential, as follows: 86.4, 84.4 and 78.1% α-amylase inhibition for the hydrolyzed proteins by Neutrase 0.8L, Alcalase 2.4L and Flavourzyme 500L, respectively. The hydrolysates obtained from enzymatic hydrolysis using the enzymes combination of Flavourzyme 500L and Alcalase 2.4L, in equal proportions, resulted in 34.7% α-glucosidase inhibition, followed by the hydrolyzed proteins produced with individual enzymes: Neutrase 0.8L (25.4% inhibition), Flavourzyme 500L (20.2% inhibition) and Alcalase 2.4L (15% inhibition). In conclusion, the results revealed that the protein hydrolysates from carioca bean can be used potential anti-diabetic agents.