Production and characterization of thermostable ?-amylase from thermophilic Anoxybacillus flavithermus sp nov SO-19

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dc.authoridDUNDAR, ABDURRAHMAN/0000-0002-7930-1054
dc.authoridDumontet, Stefano/0000-0001-8127-3120
dc.authoridOkumus, Veysi/0000-0002-5505-2700
dc.contributor.authorOzdemir, Sadin
dc.contributor.authorOkumus, Veysi
dc.contributor.authorUlutas, Mehmet Sefa
dc.contributor.authorDundar, Abdurrahman
dc.contributor.authorAkarsubasic, Alper Tunga
dc.contributor.authorDumontet, Stefano
dc.date.accessioned2024-12-24T19:24:22Z
dc.date.available2024-12-24T19:24:22Z
dc.date.issued2016
dc.departmentSiirt Üniversitesi
dc.description.abstractThis study was concerned with isolation and identification of thermophilic bacteria from hot spring in Afyonkarahisar (Gecek) and optimization of a-amylase production, partial purification of alpha-amylase, and characterization of extracellular enzyme from isolated thermophilic strain 19. To characterize and identify the thermophilic isolated bacteria, morphological analysis and biochemistry tests were studied. Besides, for classification 16S rRNA gene, G-C content and DNA-DNA hybridization analysis were performed. These results indicated that strain 19 is a novel species, Anoxybacillus flavithermus sp. nov. The effects of different fermentation conditions, such as incubation time, temperature, and pH, different carbon and nitrogen sources, and surfactants on a-amylase production were investigated. Various parameters such as temperature and temperature stability, pH and pH stability, detergents and surfactants, different starches, and metal ions on influence of enzyme characterization were assayed. About 93, 87, and 81% of the activities were retained after heating the partially purified enzyme solution at 50, 60, and 70 for 240 min, respectively. Enzyme was excessively inhibited by Hg2+ (6%). The enzyme was activated by Co2+ (212%) and Mg2+ (142%). Enzyme degradated 82% of starch content in apple juice at 70 degrees C in 30 min. The molecular weight of enzyme was estimated as 96 kDa.
dc.description.sponsorshipScientific Research Projects Unit of Siirt University, Turkey [BAP-2011-SIUFED-F3]
dc.description.sponsorshipThis study was supported by Scientific Research Projects Unit of Siirt University (project code: BAP-2011-SIUFED-F3), Turkey.
dc.identifier.doi10.1002/star.201500071
dc.identifier.endpage1253
dc.identifier.issn0038-9056
dc.identifier.issn1521-379X
dc.identifier.issue11-12
dc.identifier.scopus2-s2.0-84962670748
dc.identifier.scopusqualityQ2
dc.identifier.startpage1244
dc.identifier.urihttps://doi.org/10.1002/star.201500071
dc.identifier.urihttps://hdl.handle.net/20.500.12604/5941
dc.identifier.volume68
dc.identifier.wosWOS:000389311200025
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherWiley-V C H Verlag Gmbh
dc.relation.ispartofStarch-Starke
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_20241222
dc.subjectAnoxybacillus flavithermus
dc.subjectalpha-Amylase
dc.subjectApple juice industry
dc.subjectDetergent industry
dc.subjectThermostable
dc.titleProduction and characterization of thermostable ?-amylase from thermophilic Anoxybacillus flavithermus sp nov SO-19
dc.typeArticle

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