Abstract
Peptide composition and peptide aggregation in β-lactoglobulin (β-LG) hydrolysate were studied as related to residual chymotryptic activity in a commercial trypsin (CT) preparation. Residual chymotryptic activity produced smaller and more hydrophobic peptides in tryptic hydrolysate of β-LG, which enhanced peptide aggregation, mainly at acidic pH. The contribution of the chymotryptic peptide β-LG 15–20 to this aggregation process appeared to be very important, but other peptides (i.e., β-LG 41/43−60, 1–8 and 61−69/70+149−162) and residual α-LA may also decrease peptide solubility. When using CT mixtures in the preparation of whey protein hydrolysates, the impact of residual chymotryptic activity should not be neglected because of its influence on peptide–peptide interactions and on the resulting solubility of the hydrolyzed product.
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