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Studies on methanol-oxidizing bacteria

II. Purification and properties of methanol dehydrogenase fromPseudomonas RJ1

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Abstract

An ammonium-ion-activated, pyridine nucleotide-independent, phenazine methosulfate-linked methanol dehydrogenase has been isolated fromPseudomonas RJ1. The enzyme was purified to homogenity as judged by gel filtration, ultracentrifugation and disc gel electrophoresis. In analytical ultracentrifugation, it shows a single protein peak with an approximate molecular weight of 120 000. In polyacrylamide gel electrophoresis at pH 4.0 and at pH 0.9 it shows only one protein band. This enzyme has dual substrate specificity for normal primary alcohols and formaldehyde. It has a pH optimum of 9.0. The Km value of the enzyme was calculated to be 1.2 × 10−5 m for methanol and 1.1 × 10−5 m for ethanol.

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  1. R. J. Mehta

    Present address: Department of Microbiology, Smith Kline & French Laboratories, 1500 Spring Garden Street, 19101, Philadelphia, Pa., USA

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  1. Department of Microbiology, University of Texas, 78712, Austin, Texas, USA

    R. J. Mehta

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Mehta, R.J. Studies on methanol-oxidizing bacteria. Antonie van Leeuwenhoek 39, 303–312 (1973). https://doi.org/10.1007/BF02578862

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  • DOI: https://doi.org/10.1007/BF02578862

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