STUDIES ON THE CHARACTERIZATION OF SERINE PROTEINASE AND PANCREATIN PLASTEINS

Studies have shown that sodium caseinate plasteins realized with tryps in, alpha-chymotrypsin or a combination of both enzymes exhibit simila rities as regards their amino acid pattern and their functional proper ties, whilst the relative chain lengths of the plastein peptides and p lastein yields are differing. Plasteins obtained with pancreatin as ph ysiological enzyme system differ markedly in their composition and beh aviour from serine proteinase plasteins, which reflects the influence of the peptidases on plastein formation. High tyrosine contents (appro ximately 35 mol %) indicate that strongly hydrophobic, proteolysis-res istant, tyrosine-containing peptides are concentrated in the pancreati n plasteins.