Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation

In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-δ-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels.