Screening, partial purification and characterization of the hyper-thermophilic lipase produced by a new isolate ofBacillus subtilisLP2

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dc.authoridAKTAS, Fatih/0000-0002-2031-298X
dc.contributor.authorYasar, Gulhan
dc.contributor.authorGulhan, Unzile Guven
dc.contributor.authorGuduk, Elif
dc.contributor.authorAktas, Fatih
dc.date.accessioned2021-12-01T18:50:27Z
dc.date.available2021-12-01T18:50:27Z
dc.date.issued2020
dc.department[Belirlenecek]en_US
dc.description.abstractLipases are one of the most important catalysts for several industries such as detergent, dairy, and textile industry due to their bio-catalytic ability in aqueous and non-aqueous media. Stability to extreme conditions is an important property since it makes enzymes suitable to several industrial processes. In this study, lipase producing soil bacteria were screened and identified with 16S rDNA sequencing. A new hyper-thermophilic lipase named asBacillus subtilis LP2isolate was partially purified by ammonium sulphate precipitation with 17.8-fold purification and 583 U/mg specific activity. Maximum activity was exhibited at pH 7 and 80 degrees C with the substrate tween 80 K(M)and V(max)values were calculated as 18.3 mM and 680 U/mg with a catalytic efficiency (k(cat)/K-M) of 307 s(-1)M(-1). These results indicate that lipase fromBacillus subtilis LP2can be a valuable candidate for industrial applications such as organic synthesis and fats and oils industry due to their efficient catalysis in higher temperatures.en_US
dc.identifier.doi10.1080/10242422.2020.1751829
dc.identifier.endpage375en_US
dc.identifier.issn1024-2422
dc.identifier.issn1029-2446
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85083580043en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage367en_US
dc.identifier.urihttps://doi.org/10.1080/10242422.2020.1751829
dc.identifier.urihttps://hdl.handle.net/20.500.12684/10879
dc.identifier.volume38en_US
dc.identifier.wosWOS:000549070100004en_US
dc.identifier.wosqualityQ4en_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.subjectLipaseen_US
dc.subjecthyper-thermophilicen_US
dc.subjectBacillusen_US
dc.subjectBacillus subtilisen_US
dc.subjectcharacterisationen_US
dc.subjectIndustrial Applicationsen_US
dc.subjectBiochemical-Propertiesen_US
dc.subjectThermostable Lipaseen_US
dc.subjectAlkaline Lipaseen_US
dc.subjectBacillusen_US
dc.subjectMetallolipaseen_US
dc.subjectEnzymesen_US
dc.subjectFooden_US
dc.titleScreening, partial purification and characterization of the hyper-thermophilic lipase produced by a new isolate ofBacillus subtilisLP2en_US
dc.typeArticleen_US

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