Yeast alcohol dehydrogenase immobilized in a glutaraldehyde-albumin matrix: kinetics and cofactor diffusional effects

Journal Article · Fri May 01 00:00:00 EDT 1981 · Gasohol U.S.A.; (United States)

DOI:https://doi.org/10.1002/bit.260230506· OSTI ID:5135722

Millis, J R; Wingard, Jr, L B

Yeast alcohol dehydrogenase was immobilized in an albumin matrix crosslinked with 2.5 or 5.0% glutaraldehyde to give 102-1685/mu/m thick membranes. The enzyme half-life was at least doubled at pH 7.5 or 8.8 on immobilization. Values of the kinetic constants for the soluble and immobilized enzyme were determined at 25/degree/C and pH 8.8 over the range of 0.01-1.0M bulk solution concentration of ethanol as substrate and 140-1000/mu/M bulk solution concentration of nicotinamide adenine dinucleotide (NAD/sup +/) as cofactor. The four kinetic constants for the soluble enzyme increased with immobilization of the enzyme. The Michaelis constants for NAD/sup +/ and for ethanol were greater for the immobilized enzyme. The diffusional resistance to NAD/sup +/ transport, presented in terms of the Thiele modulus, showed that the overall rate of reaction was decreased by about 50% even at values of the modulus as low as 2.0. 21 refs.

• Research Organization: Univ. of Pittsburgh, PA
• OSTI ID: 5135722
• Journal Information: Gasohol U.S.A.; (United States), Vol. 23:5
• Country of Publication: United States
• Language: English

Related Subjects

10 SYNTHETIC FUELS
59 BASIC BIOLOGICAL SCIENCES
ETHANOL
BIOCHEMICAL REACTION KINETICS
IMMOBILIZED ENZYMES
PERFORMANCE
OXIDOREDUCTASES
ALBUMINS
ALDEHYDES
DIFFUSION
MEMBRANES
YEASTS
ALCOHOLS
ENZYMES
FUNGI
HYDROXY COMPOUNDS
KINETICS
MICROORGANISMS
ORGANIC COMPOUNDS
PLANTS
PROTEINS
REACTION KINETICS
090210* - Alcohol Fuels- Properties- (1976-1989)
550200 - Biochemistry