OBTENTION AND CHARACTERIZATION OF HYDROLYSATES FROM MACAUBA (Acrocomia aculeata) KERNEL PROTEIN ISOLATE

Protein hydrolysates are the product of protein hydrolysis by enzymes, which in addition to improving the physicochemical properties of proteins, leads to the generation of bioactive peptides. Peptides extracted from food proteins have attracted much attention due to their special physiological functions, such as antioxidant, hypoglycemic and antibacterial activity. The selection of enzymes plays a crucial role in the preparation of biologically active peptides, and suitable proteases can exert maximum biological activity. This study aimed to obtain hydrolysates from macauba kernel protein isolate, for the first time, using different enzymes and evaluate their antioxidant capacity. Two methods were used to obtain hydrolysates, one simulating gastrointestinal digestion (HD), using the enzymes pepsin (1:20) and pancreatin (1:20), and the other one using alcalase (HA) at 1% by mass of protein. Protein profile of the hydrolysates was determined by SDS-PAGE. Antioxidant capacity was assessed using the ABTS method. MKPI was used as a control for all analyses. Gel electrophoresis indicated that after hydrolysis there was no protein larger than 20 kDa. Proteins were below 15 and 20 kDa for HD and HA, respectively. MKPI showed proteins with molecular weight up to 60 kDa, indicating the effectiveness of enzymes in hydrolyzing MKPI. In addition, HD had a higher antioxidant capacity than HA (8.52 ± 0.47 and 3.19 ± 0.15 mg eq TE/mL, respectively), but both were higher than MKPI (0.12 ± 0.024 mg eq TE/mL). Thus, this work presents unique information related to hydrolysates from macauba kernels with antioxidant activity and potentially containing bioactive peptides, in which hydrolysis simulating gastrointestinal digestion (HD) showed a higher concentration of smaller proteins (15 kDa) and higher antioxidant capacity. Future work must further identify the peptides with the strongest biological activity and determine the mechanism of action for their actual efficacy.