The Production of Functional Peptide from Whey Using Immobilized Trypsin

Carbohydrate-free caseinomacropeptide (CMP) was isolated from the sweet whey powder by a precipitation method using 12% trichloroacetic acid. The yield of carbohydrate-free CMP was 2.7 g from 100 g sweet whey powder. The electrophoretic pattern and the amino acid analysis of CMP showed that isolated CMP was quite pure, indicating the precipitation with 12% trichloroacetic acid was very effective for isolating carbohydrate-free CMP from the sweet whey powder. Trypsin, covalently immobilized on pore glass beads by carbodiimide (EDC) method, was 20mg per 1g glass beads. CMP was almost completely hydrolyzed by soluble trypsin in 24hr, but not by immobilized trypsin. The tryptic hydrolysates were fractionated on a Bio-Gel P 4 column and separated peptides were tested for their capacities to inhibit platelet aggregation using a aggregometer. The hydrolysate obtained from CMP after 24hr digestion by immobilized trypsin showed the highest activity.