文摘
Tripeptide was produced during the permeation of a gelatin solution through the poreof a collagenase-immobilized porous hollow-fiber membrane. Gelatin was obtained viahydrolysis of fish collagen. First, an epoxy-group-containing monomer was graft-polymerized onto an electron-beam-irradiated porous hollow-fiber membrane. Second,the 2-hydroxyethylamino group was introduced into the epoxy group to bind collagenaseon the basis of electrostatic interaction. Third, adsorbed collagenase was cross-linkedwith glutaraldehyde to prevent leakage of the enzyme. Gelatin solution (10-50 g/L)was forced to permeate across the collagenase-immobilized porous hollow-fiber membrane with a density of immobilized collagenase of 52 mg/g at various residence timesof the gelatin solution ranging from 0.13 to 20 min. Fourteen percent in weight of 10g/L gelatin solution was hydrolyzed into tripeptide at a residence time of 20 min.