| BURYŠKA, Tomáš, Petra BABKOVÁ, Ondřej VÁVRA, Jiří DAMBORSKÝ a Zbyněk PROKOP. A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity. APPLIED AND ENVIRONMENTAL MICROBIOLOGY. American Society for Microbiology, 2018, roč. 84, č. 2, s. 1-13. ISSN 0099-2240. |
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@article{1402018,
author = {Buryška, Tomáš and Babková, Petra and Vávra, Ondřej and Damborský, Jiří and Prokop, Zbyněk},
article_number = {2},
keywords = {biotechnology; cosolvents; enzyme; haloalkane dehalogenase; marine; microbial; stability; substrate specificity},
language = {eng},
issn = {0099-2240},
journal = {APPLIED AND ENVIRONMENTAL MICROBIOLOGY},
title = {A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity},
volume = {84},
year = {2018}
}
TY - JOUR
ID - 1402018
AU - Buryška, Tomáš - Babková, Petra - Vávra, Ondřej - Damborský, Jiří - Prokop, Zbyněk
PY - 2018
TI - A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity
JF - APPLIED AND ENVIRONMENTAL MICROBIOLOGY
VL - 84
IS - 2
SP - 1-13
EP - 1-13
PB - American Society for Microbiology
SN - 00992240
KW - biotechnology
KW - cosolvents
KW - enzyme
KW - haloalkane dehalogenase
KW - marine
KW - microbial
KW - stability
KW - substrate specificity
N2 - 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.
ER -
BURYŠKA, Tomáš, Petra BABKOVÁ, Ondřej VÁVRA, Jiří DAMBORSKÝ a Zbyněk PROKOP. A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity. \textit{APPLIED AND ENVIRONMENTAL MICROBIOLOGY}. American Society for Microbiology, 2018, roč.~84, č.~2, s.~1-13. ISSN~0099-2240.
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