Production of Tripeptide from Gelatin Using Collagenase-Immobilized Porous Hollow-Fiber Membrane

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Abstract
Tripeptide was produced during the permeation of a gelatin solution through the pore of a collagenase‐immobilized porous hollow‐fiber membrane. Gelatin was obtained via hydrolysis 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 collagenase on the basis of electrostatic interaction. Third, adsorbed collagenase was cross‐linked with 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 times of the gelatin solution ranging from 0.13 to 20 min. Fourteen percent in weight of 10 g/L gelatin solution was hydrolyzed into tripeptide at a residence time of 20 min.