Immobilization of enzyme onto poly(ethylene-vinyl alcohol) membrane

Journal Article · Sat Feb 01 00:00:00 EST 1986 · Biotechnol. Bioeng.; (United States)

DOI:https://doi.org/10.1002/bit.260280208· OSTI ID:5328213

Imai, K; Shiomi, T; Uchida, K; Miya, M

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, Km, was smaller for invertase bound by APA with longer molecular lengths than for invertase bound by AAA. We attempted to bind glucoamylase of Rhizopus delemarorigin in the same way. The amount and activity of immobilized glucoamylase were much less than those of invertase. 16 references.

• Research Organization: Tech Univ. Nagaoka, Niigata, Japan
• OSTI ID: 5328213
• Journal Information: Biotechnol. Bioeng.; (United States), Vol. 28:2
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
09 BIOMASS FUELS
IMMOBILIZED ENZYMES
CHEMICAL PREPARATION
PHYSICAL PROPERTIES
O-GLYCOSYL HYDROLASES
BIOCHEMICAL REACTION KINETICS
AMYLASE
IONS
MEMBRANES
PH VALUE
RHIZOPUS
STABILITY
CHARGED PARTICLES
ENZYMES
FUNGI
GLYCOSYL HYDROLASES
HYDROLASES
KINETICS
PLANTS
REACTION KINETICS
SYNTHESIS
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