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Immobilization of enzymes by radiopolymerization of acrylamide
Author(s) -
Kawashima Koji,
Umeda Keiji
Publication year - 1974
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260160505
Subject(s) - acrylamide , invertase , chemistry , glucose oxidase , starch , enzyme , immobilized enzyme , amylase , chromatography , biochemistry , organic chemistry , polymer , copolymer
A new and simple method for immobilization of enzymes by the aerobic radio‐polymerization of acrylamide was developed. Irradiation treatment of acrylamide in the frozen state produces a spongy immobilized enzyme membrane without the addition of carriers. Aerobic polymerization yields of acrylamide in the frozen state were increased by the addition of starch and also by lyophilization. Glucose oxidase (activity recovery was 12.3–33.7%), invertase (69.2%), D ‐amono acid oxidase (25.0–70.5%), aminoacylase (39.2–43.7%), mold α‐amylase (18.0%), malt β‐amylase (4.1%), glucoamylase (6.5%), alkaline protease (5.3%), and neutral protease (10.5%) were immobilized by this method. Invertase entrapped by this method had a wider optium pH range and was active at higher temperatures.