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Yeast alcohol dehydrogenase structure and catalysis. [PDF]
Biochemistry, 2014 Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different
Raj SB, Ramaswamy S, Plapp BV.
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High-Throughput Screening of Industrial Brewing Yeast with Lower Synthetic Level of Acetaldehyde During Beer Production [PDF]
FoodsThe high level of acetaldehyde produced by yeast is a significant concern for all enterprises of beer production. To obtain industrial beer yeast strains with low ability to produce acetaldehyde, a multi-step screening strategy was established, using ...
Shuangxin Han +9 more
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Immobilization and stabilization of alcohol dehydrogenase on polyvinyl alcohol fibre [PDF]
Biotechnology Reports, 2018 A polyvinyl alcohol (PVA) fibrous carrier has been chemically modified for the immobilization of yeast alcohol dehydrogenase (ADH) with an aim to increase its stability over a wide pH range, prolong its activity upon storage, and enhance its reusability.
Priydarshani Shinde +4 more
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Binding of coenzymes to yeast alcohol dehydrogenase [PDF]
Journal of the Serbian Chemical Society, 2010 In this work, the binding of coenzymes to yeast alcohol dehydrogenase (EC 1.1.1.1) were investigated. The main criterions were the change in the standard free energies for individual reaction steps, the internal equilibrium constants and the overall ...
VLADIMIR LESKOVAC +4 more
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Protein thermal stability in the undergraduate biochemistry laboratory: Exploring protein thermal stability with yeast alcohol dehydrogenase. [PDF]
Biochem Mol Biol EducAbstract We created a novel laboratory experience where undergraduate students explore the techniques used to study protein misfolding, unfolding, and aggregation. Despite the importance of protein misfolding and aggregation diseases, protein unfolding is not typically explored in undergraduate biochemistry laboratory classes.
Bates A, Williams KM, Hagerman AE.
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Structure and function of yeast alcohol dehydrogenase [PDF]
Journal of the Serbian Chemical Society, 2000 1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10.
Trivić Svetlana, Leskovac Vladimir
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Journal of the Serbian Chemical Society, 2000 Erratum In the paper entitled "Structure and Function of Yeast Alcohol Dehydrogenase" by Svetlana Trivić and Vladimir Leskovac published in J. Serb. Chem. Soc. Vol. 65. No. 4 (2000) Table 5 on page 213 should be replaced with: TABLE V.
Editorial
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Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions [PDF]
Journal of the Serbian Chemical Society, 2003 In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25 ºC, have been estimated. The determination of the individual rate constants was achieved by fitting the
Leskovac Vladimir M. +2 more
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Recombinant yeast for production of the pain receptor modulator nonivamide from vanillin
Frontiers in Chemical Engineering, 2023 We report on the development of a method based on recombinant yeast Saccharomyces cerevisiae to produce nonivamide, a capsaicinoid and potent agonist of the pain receptor TRPV1. Nonivamide was produced in a two-step batch process where yeast was i) grown
Nina Muratovska, Magnus Carlquist
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MAGNETIC FIELD EFFECT ON YEAST Saccharomyces cerevisiae ACTIVITY AT GRAPE MUST FERMENTATION [PDF]
Biotechnologia Acta, 2013 Treatment of yeast cultures using magnetic fields enables us to gain a better understanding of the magnetic fields’ action on enzyme activity and the fluctuation of macro- and micro-element concentrations within yeast cultures.
V. N. Bayraktar
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