Comparison of the influence of pH on the selectivity of free and immobilized trypsin for β-lactoglobulin hydrolysis.

Although immobilized trypsin is a viable alternative to the free one in solution for producing protein hydrolysates, the change of selectivity introduced by immobilization is unclear. In this study, we compared the selectivity of free and immobilized trypsin towards different cleavage sites of β-lactoglobulin (β-Lg) with a focus on the impact of environmental pH. Both free and immobilized trypsin exhibited greater accessibility to native β-Lg at elevated pH (from pH 7.