Effects of Various Inhibitors on ?-galactosidase Purified from the Thermoacidophilic Alicyclobacillus acidocaldarius Subsp Rittmannii Isolated from Antarctica

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dc.contributor.authorGuven, Reyhan Gul
dc.contributor.authorKaplan, Alevcan
dc.contributor.authorGuven, Kemal
dc.contributor.authorMatpan, Fatma
dc.contributor.authorDogru, Mehmet
dc.date.accessioned2024-04-24T16:02:46Z
dc.date.available2024-04-24T16:02:46Z
dc.date.issued2011
dc.departmentDicle Üniversitesien_US
dc.description.abstractbeta-Galactosidase purified from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. rittmannii isolated from Antarctica is a member of the GH42 family. The enzyme was not effected by various concentrations of its reaction product glucose, but was greatly inhibited by the other reaction product galactose using both substrates, ONPG and lactose. Linewever-Burk plot analysis derived from both ONPG and lactose hydrolysis results showed that galactose is a mixed-type inhibitor of the purified beta-galactosidase. The enzyme was slightly activated by Mg(2+) (13% at 20 mM), while inhibited at higher concentrations of Ca(+2) (33% at 10 mM), Zn(+2) (86% at 8 mM) and Cu(+2) (87% at 4 mM). The enzyme activity was not significantly altered by the metal ion chelators EDTA and 1,10-phenanthroline up to 20 mM, indicating that this enzyme is not a metalloenzyme. 2-Mercaptoethanol and DTT were found to enhance beta-galactosidase activity, while p-chloromercuribenzoic acid (PCMB) completely inhibited enzymatic activity (97% at 1 mM; 99.7% at 2 mM), indicating at least one essential Cys residue modified by the reagents in the active site of beta-galactosidase. Iodoacetamide and N-ethylmaleimide had little effect on the beta-galactosidase. Phenylmethylsulfonyl fluoride (PMSF) inhibited the enzyme strongly (19.8% at 1 mM; 71.9% at 10 mM), also showing the participation of serine for enzyme activity.en_US
dc.identifier.doi10.1007/s12257-010-0070-7
dc.identifier.endpage119en_US
dc.identifier.issn1226-8372
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-80052027571
dc.identifier.scopusqualityQ2
dc.identifier.startpage114en_US
dc.identifier.urihttps://doi.org/10.1007/s12257-010-0070-7
dc.identifier.urihttps://hdl.handle.net/11468/14907
dc.identifier.volume16en_US
dc.identifier.wosWOS:000287959500014
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.publisherKorean Soc Biotechnology & Bioengineeringen_US
dc.relation.ispartofBiotechnology and Bioprocess Engineering
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBeta-Galactosidaseen_US
dc.subjectMetal Ion Chelatorsen_US
dc.subjectInhibitionen_US
dc.subjectGalactoseen_US
dc.subjectPmcb And Pmsfen_US
dc.titleEffects of Various Inhibitors on ?-galactosidase Purified from the Thermoacidophilic Alicyclobacillus acidocaldarius Subsp Rittmannii Isolated from Antarcticaen_US
dc.titleEffects of Various Inhibitors on ?-galactosidase Purified from the Thermoacidophilic Alicyclobacillus acidocaldarius Subsp Rittmannii Isolated from Antarctica
dc.typeArticleen_US

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