Metagenome-derived haloalkane dehalogenases with novel catalytic properties

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00477522" target="_blank" >RIV/61388971:_____/17:00477522 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14310/17:00095407

Result on the web

<a href="http://dx.doi.org/10.1007/s00253-017-8393-3" target="_blank" >http://dx.doi.org/10.1007/s00253-017-8393-3</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00253-017-8393-3" target="_blank" >10.1007/s00253-017-8393-3</a>

Result language

angličtina

Original language name

Metagenome-derived haloalkane dehalogenases with novel catalytic properties

Original language description

Haloalkane dehalogenases (HLDs) are environmentally relevant enzymes cleaving a carbon-halogen bond in a wide range of halogenated pollutants. PCR with degenerate primers and genome-walking was used for the retrieval of four HLD-encoding genes from groundwater-derived environmental DNA. Using specific primers and the environmental DNA as a template, we succeeded in generating additional amplicons, resulting altogether in three clusters of sequences with each cluster comprising 8-13 closely related putative HLD-encoding genes. A phylogenetic analysis of the translated genes revealed that three HLDs are members of the HLD-I subfamily, whereas one gene encodes an enzyme from the subfamily HLD-II. Two metagenome-derived HLDs, eHLDB and eHLD-C, each from a different subfamily, were heterologously produced in active form, purified and characterized in terms of their thermostability, pH and temperature optimum, quaternary structure, substrate specificity towards 30 halogenated compounds, and enantioselectivity. eHLD-B and eHLD-C showed striking differences in their activities, substrate preferences, and tolerance to temperature. Profound differences were also determined in the enantiopreference and enantioselectivity of these enzymes towards selected substrates. Comparing our data with those of known HLDs revealed that eHLD-C exhibits a unique combination of high thermostability, high activity, and an unusually broad pH optimum, which covers the entire range of pH 5.5-8.9. Moreover, a so far unreported high thermostability for HLDs was determined for this enzyme at pH values lower than 6.0. Thus, eHLD-C represents an attractive and novel biocatalyst for biotechnological applications.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Applied Microbiology and Biotechnology

ISSN

0175-7598

e-ISSN

—

Volume of the periodical

101

Issue of the periodical within the volume

16

Country of publishing house

DE - GERMANY

Number of pages

13

Pages from-to

6385-6397

UT code for WoS article

000407077400009

EID of the result in the Scopus database

2-s2.0-85021839578