Immobilization of enzyme into poly(vinyl alcohol) membrane

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

DOI:https://doi.org/10.1002/bit.260281116· OSTI ID:6593822

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

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 Km was larger for immobilized glucoamylase than for the native one, while Vmax was smaller for the immobilized enzyme. Also, the apparent Km appeared to be affected by the molecular size of the substrate. Further, immobilized invertase and cellulase showed good stabilities in repeating usage. 9 references.

• Research Organization: Technological Univ. of Nagaoka, Niigata, Japan
• OSTI ID: 6593822
• Journal Information: Biotechnol. Bioeng.; (United States), Vol. 28:11
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
09 BIOMASS FUELS
IMMOBILIZED ENZYMES
CHEMICAL PREPARATION
STABILITY
ALBUMINS
CATTLE
CELLULASE
DIAGRAMS
ENZYMES
EVALUATION
MEMBRANES
PH VALUE
POLYVINYLS
QUANTITY RATIO
SIZE
SODIUM COMPOUNDS
SUBSTRATES
THERMODYNAMIC PROPERTIES
ULTRAVIOLET RADIATION
ALKALI METAL COMPOUNDS
ANIMALS
DOMESTIC ANIMALS
ELECTROMAGNETIC RADIATION
GLYCOSYL HYDROLASES
HYDROLASES
MAMMALS
O-GLYCOSYL HYDROLASES
ORGANIC COMPOUNDS
ORGANIC POLYMERS
PHYSICAL PROPERTIES
POLYMERS
PROTEINS
RADIATIONS
RUMINANTS
SYNTHESIS
VERTEBRATES
550400* - Genetics
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