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

J 2018

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

BURYŠKA, Tomáš, Petra BABKOVÁ, Ondřej VÁVRA, Jiří DAMBORSKÝ, Zbyněk PROKOP et. al.

Základní údaje

Originální název

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

Autoři

BURYŠKA, Tomáš (203 Česká republika, domácí), Petra BABKOVÁ (203 Česká republika, domácí), Ondřej VÁVRA (203 Česká republika, domácí), Jiří DAMBORSKÝ (203 Česká republika, garant, domácí) a Zbyněk PROKOP (203 Česká republika, domácí)

Vydání

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, American Society for Microbiology, 2018, 0099-2240

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

20801 Environmental biotechnology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 4.077

Kód RIV

RIV/00216224:14310/18:00100776

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000419048900005

Klíčová slova anglicky

biotechnology; cosolvents; enzyme; haloalkane dehalogenase; marine; microbial; stability; substrate specificity

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 26. 2. 2018 07:51, prof. Mgr. Jiří Damborský, Dr.

Anotace

V originále

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.

Návaznosti

GA16-07965S, projekt VaV

Název: Řízená evoluce dynamických elementů v enzymech s využitím mikrofluidních čipů

Investor: Grantová agentura ČR, Řízená evoluce dynamických elementů v enzymech s využitím mikrofluidních čipů

LM2011028, projekt VaV

Název: RECETOX ? Národní infrastruktura pro výzkum toxických látek v prostředí

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, RECETOX Národní infrastruktura pro výzkum toxických látek v prostředí

LO1214, projekt VaV

Název: Centrum pro výzkum toxických látek v prostředí (Akronym: RECETOX)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum pro výzkum toxických látek v prostředí

Citovat

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.

@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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