Purification and characterization of an extracellular cellulase from Anoxybacillus gonensis O9 isolated from geothermal area in Turkey

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Özet

In the present study, cellulase was purified and characterized from Anoxybacillus gonensis (Gen bank Number: KM596794) which was isolated and characterized from Agri Diyadin Hot spring. It was found to synthesize cellulase which had a wide range of industrial applications. Twenty four-hour-cultured bacteria induced cellulase production and specific activities during the purification steps were 1.47,81.06 and 109.4 EU mg-1 protein at crude extract, ammonium sulphate precipitated and DEAE-Sephadex purification steps. The highest enzyme activity was observed at 50°C and the optimum range of pH was 3-10. Molecular weight of enzyme was determined approximately 40kDa. The kinetic parameters of cellulase against carboxymethylcellulose (CMC) were 153.4 μmol min-1 mg for Vmax and 0.46mM for Km. Among effectors of the enzyme, Zn2+, Ca2+, Co2+ and EDTA decreased enzyme activity.

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Tam Kayıt
AlanDeğerDil
dc.contributor.authorGenc, Berna
dc.contributor.authorNadaroglu, Hayrunnisa
dc.contributor.authorAdiguzel, Ahmet
dc.contributor.authorBaltaci, Ozkan
dc.date.accessioned2026-10-22T10:23:39.886062835Z
dc.date.available2026-10-22T10:23:39.886062835Z
dc.date.issued2015
dc.description.abstractIn the present study, cellulase was purified and characterized from Anoxybacillus gonensis (Gen bank Number: KM596794) which was isolated and characterized from Agri Diyadin Hot spring. It was found to synthesize cellulase which had a wide range of industrial applications. Twenty four-hour-cultured bacteria induced cellulase production and specific activities during the purification steps were 1.47,81.06 and 109.4 EU mg-1 protein at crude extract, ammonium sulphate precipitated and DEAE-Sephadex purification steps. The highest enzyme activity was observed at 50°C and the optimum range of pH was 3-10. Molecular weight of enzyme was determined approximately 40kDa. The kinetic parameters of cellulase against carboxymethylcellulose (CMC) were 153.4 μmol min-1 mg for Vmax and 0.46mM for Km. Among effectors of the enzyme, Zn2+, Ca2+, Co2+ and EDTA decreased enzyme activity.
dc.description.sponsorshipResearch Development Centre of Ataturk University
dc.description.sponsorshipAtaturk University, Turkey
dc.identifier.endpage1324
dc.identifier.issn0254-8704
dc.identifier.issue6
dc.identifier.pmid26688967
dc.identifier.scopus2-s2.0-84949454934
dc.identifier.startpage1319
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/gumushane/15159
dc.identifier.volume36
dc.identifier.wosWOS:000364799400011
dc.language.isoen
dc.publisherTriveni Enterprises
dc.relation.ispartofJournal of Environmental Biology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subject16S rRNA sequencing
dc.subjectAnoxybacillus gonensis
dc.subjectCellulase
dc.subjectCharacterization
dc.subject.classificationEnvironmental Sciences
dc.subject.classificationEnvironmental Sciences & Ecology
dc.subject.otherAnoxybacillus
dc.subject.otherCellulases
dc.subject.otherGene Expression Regulation, Bacterial
dc.subject.otherGene Expression Regulation, Enzymologic
dc.subject.otherHot Springs
dc.subject.otherKinetics
dc.subject.otherSubstrate Specificity
dc.subject.otherTemperature
dc.subject.otherAgri
dc.subject.otherDiyadin
dc.subject.otherTurkey
dc.subject.otherAnoxybacillus gonensis
dc.subject.othercellulase
dc.subject.otherenzyme
dc.subject.otherenzyme activity
dc.subject.otherpH
dc.subject.otherprotein
dc.subject.otherpurification
dc.subject.otherreaction kinetics
dc.subject.otherRNA
dc.subject.otherthermophilic bacterium
dc.subject.otherenzyme specificity
dc.subject.otherenzymology
dc.subject.othergene expression regulation
dc.subject.othergenetics
dc.subject.othermetabolism
dc.subject.otherphysiology
dc.subject.otherthermal spring
dc.titlePurification and characterization of an extracellular cellulase from Anoxybacillus gonensis O9 isolated from geothermal area in Turkey
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus18
rdl.citation.wos14
rdl.oa.statusclosed
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)