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2016 | 63 | 2 | 273-279
Article title

Characterization of a novel laccase purified from the fungus Hohenbuehelia serotina and its decolourisation of dyes

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EN
Abstracts
EN
A novel laccase was purified from the white rot fungus, Hohenbuehelia serotina, to investigate the applications of this laccase in the decoloration of various dyes. SDS-PAGE revealed a single band of this laccase corresponding to a molecular weight of approximately 57.8 kDa. The enzyme showed activity towards several substrates, the most sensitive of which was 2,2'-Azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS). The highest enzymatic activity using ABTS as a substrate was observed at pH 6.8 and 30°C. The enzyme activity was found to be significantly enhanced in the presence of Zn2+ ions and inhibited by Fe2+ ions. Moreover, SDS and β-mercaptoethanol were inhibitory, and inhibition by L-cysteine was observed while EDTA and DMSO had almost no inhibitory effect. The laccase could effectively decolorize seven different dyes within 30 minutes at 40°C.
Year
Volume
63
Issue
2
Pages
273-279
Physical description
Dates
published
2016
received
2015-06-25
revised
2015-09-22
accepted
2015-09-23
(unknown)
2015-10-24
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Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv63p273kz
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