A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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BURYŠKA Tomáš BABKOVÁ Petra VÁVRA Ondřej DAMBORSKÝ Jiří PROKOP Zbyněk

Rok publikování 2018
Druh Článek v odborném periodiku
Časopis / Zdroj APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Klíčová slova biotechnology; cosolvents; enzyme; haloalkane dehalogenase; marine; microbial; stability; substrate specificity
Popis The haloalkane dehalogenase enzyme DmmA was identified by marine metagenomic screening. Determination of its crystal structure revealed an unusually large active site compared to those of previously characterized haloalkane dehalogenases. Here we present a biochemical characterization of this interesting enzyme with emphasis on its structure-function relationships. DmmA exhibited an exceptionally broad substrate specificity and degraded several halogenated environmental pollutants that are resistant to other members of this enzyme family. In addition to having this unique substrate specificity, the enzyme was highly tolerant to organic cosolvents such as dimethyl sulfoxide, methanol, and acetone. Its broad substrate specificity, high overexpression yield (200 mg of protein per liter of cultivation medium; 50% of total protein), good tolerance to organic cosolvents, and a broad pH range make DmmA an attractive biocatalyst for various biotechnological applications.
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