Publication details

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

Authors

BURYŠKA Tomáš BABKOVÁ Petra VÁVRA Ondřej DAMBORSKÝ Jiří PROKOP Zbyněk

Type Article in Periodical
Magazine / Source APPLIED AND ENVIRONMENTAL MICROBIOLOGY
MU Faculty or unit

Faculty of Science

Citation
Keywords biotechnology; cosolvents; enzyme; haloalkane dehalogenase; marine; microbial; stability; substrate specificity
Description 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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