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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. 1981. "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 = 1981,
month =
}
  • 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 ethanolmore » 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.« less
  • A Sequential Injection (SI) system was used to analyze the ethanol concentration in fermentation broth. The method is based on the use of immobilized NAD{sup +} dependent alcohol dehydrogenase. A non-linear standard curve for ethanol (range 0.25-100 mM) was used to determine the concentration in fermentation broth and the results correlated well with HPLC measurements. The assay time was 140 s, 0.5 {mu}mol of cofactor was used for each determination, and the relative standard deviation was less than 6% when analyzing fermentation samples. The assay system is very stable and makes it possible to reduce the cofactor consumption while keepingmore » the system set up simple.« less
  • Construction of a pilot alcohol plant has been completed in Japan to test a new idea in fermentation that could cut the time required from three or four days to several hours. According to developers, the key is an unidentified radiation-cured polymer that is used to immobilize yeast, permitting the process to run continuously.