Abstract
This study examined the production of protein hydrolysates with controlled composition from cheese whey proteins. Cheese whey was characterized and several hydrolysis experiments were made using whey proteins and purified β-lactoglobulin, assubstrates, and trypsin and α-chymotrypsin, as catalysts, at two tem peratures and several enzyme concentrations. Maximum degrees of hydrolysis obtained experimentally were compared to the theoretical values and peptide compositions were calculated. For trypsin, 100% of yield was achieved; for α-chymotrypsin, hydrolysis seemed to be dependent on the oligopeptide size. The results showed that the two proteases could hydrolyze β-lactoglobulin. Trypsin and α-chymotrypsin were stable at 40°C, but a sharp decrease in the protease activity was observed at 55°C.
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Galvão, C.M.A., Souza Silva, A.F., Custódio, M.F. et al. Controlled hydrolysis of cheese whey proteins using trypsin and α-chymotrypsin. Appl Biochem Biotechnol 91, 761–776 (2001). https://doi.org/10.1385/ABAB:91-93:1-9:761
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DOI: https://doi.org/10.1385/ABAB:91-93:1-9:761