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Bacterial 2,3-butanediol dehydrogenases.

H Höhn-Bentz, F Radler

    Archives of Microbiology
    |February 1, 1978
    PubMed
    Summary

    Microbial butanediol dehydrogenases exhibit stereoselectivity, producing either meso- or optically active butanediol. Enzymes from Bacillus polymyxa and Serratia marcescens were purified and characterized, revealing distinct kinetic and optimal conditions for their respective butanediol enantiomers.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Microbiology

    Background:

    • Butanediol dehydrogenases (BDHs) are crucial enzymes in microbial metabolism.
    • Different microorganisms possess distinct BDHs, leading to varied stereochemical outcomes in butanediol production.
    • Understanding the properties of these enzymes is vital for biotechnological applications.

    Purpose of the Study:

    • To investigate the stereoselectivity of butanediol dehydrogenases from various microbial sources.
    • To purify and characterize D(-)-butanediol dehydrogenase from Bacillus polymyxa and L(+)-butanediol dehydrogenase from Serratia marcescens.
    • To determine the kinetic parameters and optimal conditions for these purified enzymes.

    Main Methods:

    • Enzyme purification using standard biochemical techniques (e.g., fold purification, specific activity determination).
    • Enzyme characterization including determination of optimal pH, temperature, molecular weight, and kinetic parameters (Km values).
    • Spectrophotometric assays for enzyme activity using various substrates and cofactors (NAD/NADH).

    Main Results:

    • Microorganisms with L(+)-BDH predominantly produced meso-butanediol, while those with D(-)-BDH produced more optically active butanediol.
    • Purified D(-)-BDH from B. polymyxa showed optimal activity at pH 9 (oxidation) and 60°C, with specific Km values for substrates.
    • Purified L(+)-BDH from S. marcescens exhibited optimal activity at pH 9 (oxidation) and 32-36°C, with distinct Km values and substrate preferences.

    Conclusions:

    • Microbial butanediol dehydrogenases display significant stereospecificity in butanediol synthesis.
    • The characterized enzymes from B. polymyxa and S. marcescens possess distinct biochemical properties, influencing their catalytic efficiency and substrate range.
    • These findings contribute to the understanding of microbial stereoselective synthesis and have implications for chiral compound production.

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