Decolorization and detoxification of textile wastewaters by recombinant Myceliophthora thermophila and Trametes trogii laccases

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00498656" target="_blank" >RIV/61388963:_____/18:00498656 - isvavai.cz</a>

Alternative codes found

RIV/67985823:_____/18:00498684

Result on the web

<a href="http://dx.doi.org/10.1007/s13205-018-1525-3" target="_blank" >http://dx.doi.org/10.1007/s13205-018-1525-3</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s13205-018-1525-3" target="_blank" >10.1007/s13205-018-1525-3</a>

Result language

angličtina

Original language name

Decolorization and detoxification of textile wastewaters by recombinant Myceliophthora thermophila and Trametes trogii laccases

Original language description

Laccases are multi-copper oxidoreductases with broad biotechnological applications. Here, we report detailed biochemical characterization of purified recombinant laccases originating from Myceliophthora thermophila (MtL) and Trametes trogii (TtL). We identified optimal conditions for decolorization of commercial dyes and textile wastewater samples. We also tested the toxicity of decolorized wastewater samples using human peripheral blood mononuclear cells. MtL and TtL were expressed in Saccharomyces cerevisiae, and secreted enzymes were purified by consecutive hydrophobic and gel chromatography. The molecular masses of TtL (similar to 65kDa) and MtL (>100kDa) suggested glycosylation of the recombinant enzymes. Deglycosylation of MtL and TtL led to 25% and 10% decreases in activity, respectively. In a thermal stability assay, TtL retained 61% and MtL 86% of the initial activity at 40 degrees C. While TtL retained roughly 50% activity at 60 degrees C, MtL lost stability at temperatures higher than 40 degrees C. MtL and TtL preferred syringaldazine as a substrate, and the catalytic efficiencies for ABTS oxidation were 7.5 times lower than for syringaldazine oxidation. In the presence of the mediator HBT, purified TtL almost completely decolorized dyes within 30min and substantially decolorized wastewater samples from a textile factory (up to 74%) within 20h. However, products of TtL-catalyzed decolorization were more toxic than MtL-decolorized products, which were almost completely detoxified.

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

<a href="/en/project/LO1302" target="_blank" >LO1302: InterBioMed</a><br>

Continuities

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

Publication year

2018

Confidentiality

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

Name of the periodical

3 Biotech

ISSN

2190-572X

e-ISSN

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Volume of the periodical

8

Issue of the periodical within the volume

12

Country of publishing house

DE - GERMANY

Number of pages

13

Pages from-to

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UT code for WoS article

000451750800001

EID of the result in the Scopus database

2-s2.0-85057565499