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Immobilization of Enzyme into Poly(vinyl alcohol) Membrane
Author(s) -
Imai Kiyokazu,
Shiomi Tomoo,
Uchida Kozo,
Miya Masamitsu
Publication year - 1986
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.260281116
Subject(s) - vinyl alcohol , chemistry , cellulase , invertase , membrane , immobilized enzyme , substrate (aquarium) , enzyme , thermal stability , chromatography , bovine serum albumin , alcohol , nuclear chemistry , biochemistry , organic chemistry , polymer , biology , ecology
Abstract Glucoamylase, invertase, and cellulase were entrapped within poly(vinyl alcohol) (PVA) membrane cross‐linked by means of irradiation of ultraviolet light. The conditions for immobilization of glucoamylase were examined with respect to enzyme concentration in PVA, sensitizer (sodium benzoate) concentration in PVA, irradiation time, and membrane thickness. Various characteristics of immobilized glucoamylase were evaluated. Among them, the pH activity curve for the immobilized enzyme was superior to that for the native one, and thermal stability was improved by immobilization with bovine albumin. The apparent K m was larger for immobilized glucoamylase than for the native one, while V max was smaller for the immobilized enzyme. Also, the apparent K m appeared to be affected by the molecular size of the substrate. Further, immobilized invertase and cellulase showed good stabilities in repeating usage.