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

Journal Article · Sat Feb 01 04:00:00 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), Journal Name: Biotechnol. Bioeng.; (United States) Vol. 28:2; ISSN BIBIA
• Country of Publication: United States
• Language: English

Related Subjects

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