Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp isolate ANT-6

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dc.authoridCoral, Gokhan/0000-0002-3533-118X
dc.authoridAYGAN, ASHABIL/0000-0003-4936-9872
dc.contributor.authorBurhan, A
dc.contributor.authorNisa, U
dc.contributor.authorGökhan, C
dc.contributor.authorÖmer, C
dc.contributor.authorAshabil, A
dc.contributor.authorOsman, G
dc.date.accessioned2024-09-18T20:02:50Z
dc.date.available2024-09-18T20:02:50Z
dc.date.issued2003
dc.departmentHatay Mustafa Kemal Üniversitesien_US
dc.description.abstractA thermostable alkaline a-amylase producing Bacillus sp. ANT-6 was isolated from soil samples. Enzyme synthesis occurred at temperatures between 25 and 45 degreesC with an optimum of 37 degreesC. There was a slight variation in amylase synthesis within the pH range 7 and 11 with an optimum pH of 9. The optimum temperatures for amylase production and growth were the same. Analyses of the enzyme by sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed a single band, which show amylolytic activity, detected in starch gel. The relative molecular mass of the partial purified enzyme was estimated to be 94 500 Da. The enzyme showed optimum activity at pH 10.5 and 80 degreesC. The partial purified enzyme was highly active in the alkaline range of pH (9.5-13), and it was completely active up to 100 degreesC retaining 85.5% initial activity at pH 10.5. Enzyme activity was enhanced in the presence of 5 mM CaCl2 (110%) and 3 mM PMSF (103%), and inhibition with 5 mM by Zn, Na, Na-sulphide, EDTA (10 mM), Urea (8 M) and SDS (0.1%) was obtained 36.9, 21.5, 22.2, 4.90, 86% and 10.27, respectively. The enzyme was stable (55%) at high alkaline pH for 24 h. So our result showed that the enzyme was both alkaline, thermostable, thermopile and chelator resistant. The ANT-6 amylase enzyme may be suitable in liquefaction of starch, in detergent and textile industries and in other industrial applications. (C) 2003 Elsevier Science Ltd. All rights reserved.en_US
dc.identifier.doi10.1016/S0032-9592(03)00037-2
dc.identifier.endpage1403en_US
dc.identifier.issn1359-5113
dc.identifier.issn1873-3298
dc.identifier.issue10en_US
dc.identifier.scopus2-s2.0-0038613858en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1397en_US
dc.identifier.urihttps://doi.org/10.1016/S0032-9592(03)00037-2
dc.identifier.urihttps://hdl.handle.net/20.500.12483/8052
dc.identifier.volume38en_US
dc.identifier.wosWOS:000183778100002en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier Sci Ltden_US
dc.relation.ispartofProcess Biochemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBacillus sp.en_US
dc.subjectalpha-amylaseen_US
dc.subjectthermophileen_US
dc.subjectalkaliphilicen_US
dc.subjectthermostableen_US
dc.subjectchelator resistanten_US
dc.titleEnzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp isolate ANT-6en_US
dc.typeArticleen_US

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