Purification and some characterization of an extracellular ?-amylase from a thermotolerant Bacillus subtilis

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dc.contributor.authorUyar, F
dc.contributor.authorBaysal, Z
dc.contributor.authorDogru, M
dc.date.accessioned2024-04-24T17:37:53Z
dc.date.available2024-04-24T17:37:53Z
dc.date.issued2003
dc.departmentDicle Üniversitesien_US
dc.description.abstractExtracellular alpha-amylase from Bacillus subtilis was purified by ion-exchange chromatography and gel filtration. The molecular weight was determined to be 48.000. Various metal ions inhibited alpha-amylase activity even at low concentrations (5 mM). Ca2+, Ba2+, m,(2+) and Ni2+ were mild inhibitors, whereas Zn2+, Fe2+, Pb2+, H2+ Mg2+, Cd2+ and Cu2+ were potent inhibitors. The activity of the enzyme was reduced by Ca2+ at high concentrations but increased at 2.5 mM. Ethylenediaminetetraacedicacid (EDTA) also affected the enzyme activity even when compared with Ca2+ ions at low concentrations. Calcium and EDTA showed dose-dependent inhibition. Different enzyme solution containing Ca2+, Ba2+ and Mg2+ (2.5 mM and 10 mM) was added 2.5 mM EDTA and enzyme activity increased at 10 mM metal ions concentrations. The K-m and V-max values for alpha-amylase were found to be 2.2 x 10(-4) g mL(-1) and 0.020 U mL(-1), 2.91 x 10(-4) g mL(-1) and 0.016 U mL(-1), 4.04 x 10(-4) g mL(-1) and 0.021 U mL(-1) for starch, amylose and glycogen. respectively.en_US
dc.identifier.endpage322en_US
dc.identifier.issn1590-4261
dc.identifier.issn1869-2044
dc.identifier.issue3en_US
dc.identifier.scopus2-s2.0-0348219079
dc.identifier.scopusqualityQ2
dc.identifier.startpage315en_US
dc.identifier.urihttps://hdl.handle.net/11468/21229
dc.identifier.volume53en_US
dc.identifier.wosWOS:000186028200006
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofAnnals of Microbiology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBacillus Subtilisen_US
dc.subjectAlpha-Amylase Productionen_US
dc.subjectMetal Ionsen_US
dc.titlePurification and some characterization of an extracellular ?-amylase from a thermotolerant Bacillus subtilisen_US
dc.titlePurification and some characterization of an extracellular ?-amylase from a thermotolerant Bacillus subtilis
dc.typeArticleen_US

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