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Title: Stability of immobilized yeast alcohol dehydrogenase

Abstract

The effects of substrate on stabilities of native (NA) and three kinds of immobilized yeast alcohol dehydrogenase (IMA), namely PGA (the carrier; porous glass), SEA (agarose gel) prepared covalently, and AMA (anion-exchange resin) prepared ionically, were studied. The following results were obtained. 1) The deactivations of NA and IMA free from the substrate or in the presence of ethanol obey the first-order kinetics, whereas, in the presence of butyraldehyde, their deactivation behaviors are explained on the basis of coexistence of two components of YADHs, namely the labile E1 and the comparatively stable E2, with different first-order deactivation constants. (2) A few attempts for stabilization of IMA were carried out from the viewpoint of the effects of crosslinkages among the subunits of YADH for PGA and the multibonding between the carrier and enzyme for SEA. The former is effective for the stabilization, whereas the latter is not. (Refs. 19).

Authors:
; ;
Publication Date:
Research Org.:
Dept. Applied Chemistry, Faculty of Engineering, Osaka City Univ., Osaka 558, Japan
OSTI Identifier:
5348296
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biotechnol. Bioeng.; (United States); Journal Volume: 23:12
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; IMMOBILIZED ENZYMES; STABILIZATION; COENZYMES; ENZYMES; ETHANOL; OXIDOREDUCTASES; SUBSTRATES; YEASTS; ALCOHOLS; FUNGI; HYDROXY COMPOUNDS; MICROORGANISMS; ORGANIC COMPOUNDS; PLANTS; 140504* - Solar Energy Conversion- Biomass Production & Conversion- (-1989); 090222 - Alcohol Fuels- Preparation from Wastes or Biomass- (1976-1989); 550700 - Microbiology; 550200 - Biochemistry

Citation Formats

Ooshima, H., Genko, Y., and Harano, Y. Stability of immobilized yeast alcohol dehydrogenase. United States: N. p., 1981. Web. doi:10.1002/bit.260231218.
Ooshima, H., Genko, Y., & Harano, Y. Stability of immobilized yeast alcohol dehydrogenase. United States. doi:10.1002/bit.260231218.
Ooshima, H., Genko, Y., and Harano, Y. Tue . "Stability of immobilized yeast alcohol dehydrogenase". United States. doi:10.1002/bit.260231218.
@article{osti_5348296,
title = {Stability of immobilized yeast alcohol dehydrogenase},
author = {Ooshima, H. and Genko, Y. and Harano, Y.},
abstractNote = {The effects of substrate on stabilities of native (NA) and three kinds of immobilized yeast alcohol dehydrogenase (IMA), namely PGA (the carrier; porous glass), SEA (agarose gel) prepared covalently, and AMA (anion-exchange resin) prepared ionically, were studied. The following results were obtained. 1) The deactivations of NA and IMA free from the substrate or in the presence of ethanol obey the first-order kinetics, whereas, in the presence of butyraldehyde, their deactivation behaviors are explained on the basis of coexistence of two components of YADHs, namely the labile E1 and the comparatively stable E2, with different first-order deactivation constants. (2) A few attempts for stabilization of IMA were carried out from the viewpoint of the effects of crosslinkages among the subunits of YADH for PGA and the multibonding between the carrier and enzyme for SEA. The former is effective for the stabilization, whereas the latter is not. (Refs. 19).},
doi = {10.1002/bit.260231218},
journal = {Biotechnol. Bioeng.; (United States)},
number = ,
volume = 23:12,
place = {United States},
year = {Tue Dec 01 00:00:00 EST 1981},
month = {Tue Dec 01 00:00:00 EST 1981}
}