The degradation of bovine β-casein by plasmin was used as a model system to investigate the applicability of an enzyme recycle reactor for the continuous production and isolation of peptide fractions. A simple, ultrafiltration-type membrane reactor was used incorporating a commercially available hollow-fiber module normally employed for dialysis purposes (artificial kidney). The results were compared with those obtained in a batch reactor process, using HPLC to monitor the course of proteolysis.
Peptide fragments were isolated and were characterized using amino-acid analysis and N-terminal end-group determination. Sixteen peptide fragments were identified, which together accounted for virtually all the potential cleavage sites in β-casein. In the system studied the N-terminal half of β-casein appeared to be more sensitive to plasmic hydrolysis than the rest of the molecule.