Production of tripeptide from gelatin using collagenase-immobilized porous hollow-fiber membrane.
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.
Fujita
Ayako
A
Department of Materials Technology, Chiba University, 1-33 Yayoi, Inage, Chiba 263-8522, Japan.
Kawakita
Hidetaka
H
Saito
Kyoichi
K
Sugita
Kazuyuki
K
Tamada
Masao
M
Sugo
Takanobu
T
D000327:Adsorption; D003094:Collagen / Q000737:chemistry*; D017364:Collagenases / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry; D005780:Gelatin / Q000737:chemistry*; D008567:Membranes, Artificial; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D010539:Permeability; D016062:Porosity
D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D009842:Oligopeptides; D010455:Peptides; C088188:glycyl-prolyl-hydroxyproline; D005780:Gelatin; D003094:Collagen; D017364:Collagenases