Partial purification and characterization of the novel halotolerant and alkalophilic laccase produced by a new isolate of Bacillus subtilis LP2

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dc.contributor.authorYaşar, Gülhan
dc.contributor.authorGuven, Ünzile Gülhan
dc.contributor.authorGüdük, Elif
dc.contributor.authorAktaş, Fatih
dc.date.accessioned2020-04-30T23:20:34Z
dc.date.available2020-04-30T23:20:34Z
dc.date.issued2019
dc.departmentDÜ, Mühendislik Fakültesi, Çevre Mühendisliği Bölümüen_US
dc.descriptionAKTAS, Fatih/0000-0002-2031-298X; Guduk, Elif/0000-0002-9724-0566en_US
dc.descriptionWOS: 000469025700004en_US
dc.description.abstractLaccases (benzenediol: oxygen oxidoreductases, [EC1.10.3.2] are mostly known as members of the blue multicopper oxidase family that are used in very different industrial applications: textile, pulp and paper, food, cosmetics industries, bioremediation process, biosensor, biofuel and organic synthesis. Stability against the extreme conditions is an important property and it makes laccase suitable for several industrial processes. Laccase should have salt resistance to be used in textile dye degradation because the textile wastewaters include dyes with high concentrations of salts, especially NaCl. Bacterial laccases are preferable to be used for bioremediation process due to their high stability to extremely salt contaminated and alkalophilic environment. Bacillus subtilis LP2 was identified as a source of alkali-tolerant, salt resistant laccase. Laccase showed activity over a wide pH (4-10) and temperature (30-80 degrees C) range. Maximum laccase activity was observed as 140.4U/mg (umol/min*mg) at pH 8 and 50 degrees C with the substrate guaiacol. Stability of laccase was determined as 60% and 20% after incubation of the enzyme for different time intervals of 20 and 40min at 50 degrees C and pH 8. SDS (10mM) and EDTA (5mM) decreased laccase activity from 100% to 0% and 56%, respectively. Despite the other inhibitors, NaCI increased the activity of laccase to 167% at 500mM concentration. Laccase from Bacillus subtilis LP2 barely showed the activity on the substrates vanillin and L-tyrosine. These results clearly show that laccase from Bacillus subtilis LP2 has high potential to be used for several applications in textile industry.en_US
dc.description.sponsorshipKOSGEB (Small and Medium Enterprises Development Organization, Republic of Turkey); DAMAR Chemical Industry and Foreign Trade Inc.en_US
dc.description.sponsorshipThis work was supported financially by the KOSGEB (Small and Medium Enterprises Development Organization, Republic of Turkey) and DAMAR Chemical Industry and Foreign Trade Inc.en_US
dc.identifier.doi10.1080/10242422.2019.1594790en_US
dc.identifier.endpage277en_US
dc.identifier.issn1024-2422
dc.identifier.issn1029-2446
dc.identifier.issue4en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage268en_US
dc.identifier.urihttps://doi.org/10.1080/10242422.2019.1594790
dc.identifier.urihttps://hdl.handle.net/20.500.12684/4032
dc.identifier.volume37en_US
dc.identifier.wosWOS:000469025700004en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.ispartofBiocatalysis And Biotransformationen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectLaccaseen_US
dc.subjectBacillus subtilis LP2en_US
dc.subjecthalotoleranten_US
dc.subjectalkalophilicen_US
dc.subjectbioremediationen_US
dc.titlePartial purification and characterization of the novel halotolerant and alkalophilic laccase produced by a new isolate of Bacillus subtilis LP2en_US
dc.typeArticleen_US

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