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Decolorization of dyes by a novel sodium azide-resistant spore laccase from a halotolerant bacterium, Bacillus safensis sp. strain S31
Author(s) -
Maryam Siroosi,
Mohammad Ali Amoozegar,
Khosro Khajeh,
Bahareh Dabirmanesh
Publication year - 2018
Publication title -
water science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.406
H-Index - 137
eISSN - 1996-9732
pISSN - 0273-1223
DOI - 10.2166/wst.2018.281
Subject(s) - laccase , chemistry , sodium azide , abts , nuclear chemistry , spore , halotolerance , microbiology and biotechnology , bacteria , enzyme , organic chemistry , dpph , biology , genetics , antioxidant
The aim of this work was to find a new stable laccase against inhibitors and study the decolorization ability of free and immobilized laccase on different classes of dyes. Spores from a halotolerant bacterium, Bacillus safensis sp. strain S31, isolated from soil samples from a chromite mine in Iran showed laccase activity with maximum activity at 30 °C and pH 5.0 using 2, 2-azino-bis (3-ethylbenzothiazoline-6-sulfonate) (ABTS) as the substrate. The enzyme retained about 60% of its initial activity in the presence of 10% (v v -1 ) methanol, ethanol, and acetone. In contrast to many other laccases, NaN 3 , at 0.1 and 1 mM concentrations, showed a slight inhibitory effect on the enzyme activity. Also, the spore laccase (8 U l -1 ) decolorized malachite green, toluidine blue, and reactive black 5 at acidic pH values; the highest decolorization percent was 75% against reactive black 5. It was observed that addition of ABTS as a redox mediator enhanced the decolorization activity. Furthermore, immobilized spore laccase encased in calcium alginate beads decolorized 95% of reactive black 5 in the absence of mediators. Overall, this isolated spore laccase might be a potent enzyme to decolorize dyes in polluted wastewaters, especially those containing metals, salts, solvents, and sodium azide.

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