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Immobilization of enzyme onto poly(ethylene–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.260280208
Subject(s) - invertase , vinyl alcohol , chemistry , immobilized enzyme , michaelis–menten kinetics , propionaldehyde , ionic strength , membrane , alcohol , enzyme , ethylene , chromatography , polymer chemistry , organic chemistry , ethanol , enzyme assay , biochemistry , polymer , acetaldehyde , catalysis , aqueous solution
Invertase was ionically bound to the poly(ethylene–vinyl alcohol) membrane surface modified with two aminoacetals with different molecular length, 2‐dimethyl‐aminoacetoaldehyde dimethylacetal (AAA) and 3‐( N , N ‐dimethylamino‐ n ‐propanediamine) propionaldehyde dimethylacetal (APA). Immobilization conditions were determined with respect to enzyme concentration in solution, pH value, ionic strength in immobilization solution, and immobilization time. Various properties of immobilized invertase were evaluated, and thermal stability was found especially to be improved by immobilization. The apparent Michaelis constant, K m , was smaller for invertase bound by APA with longer molecular lengths than for invertase bound by AAA. We attempted to bind glucoamylase of Rhizopus delemar origin in the same way. The amount and activity of immobilized glucoamylase were much less than of invertase.