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

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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.accessioned14.07.201910:50:10
dc.date.accessioned2019-07-16T20:43:59Z
dc.date.available14.07.201910:50:10
dc.date.available2019-07-16T20:43:59Z
dc.date.issued2016
dc.departmentMAÜ, Meslek Yüksekokulları, Sağlık Hizmetleri Meslek Yüksekokulu, Tıbbi Hizmetler ve Teknikler Bölümüen_US
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.en_US
dc.description.sponsorshipScientific Research Projects Unit of Siirt University, Turkey [BAP-2011-SIUFED-F3]en_US
dc.description.sponsorshipThis study was supported by Scientific Research Projects Unit of Siirt University (project code: BAP-2011-SIUFED-F3), Turkey.en_US
dc.identifier.citationÖzdemir, S., Okumus, V., Ulutas, M. S., Dundar, A., Akarsubasic, A. T., & Dumontet, S. (2016). Production and characterization of thermostable α-amylase from thermophilicAnoxybacillus flavithermussp. nov. SO-19. Starch - Stärke, 68(11–12), 1244–1253. https://doi.org/10.1002/star.201500071
dc.identifier.doi10.1002/star.201500071en_US
dc.identifier.endpage1253en_US
dc.identifier.issn0038-9056
dc.identifier.issn1521-379X
dc.identifier.issue11.Decen_US
dc.identifier.scopus2-s2.0-84962670748en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1244en_US
dc.identifier.urihttps://dx.doi.org/10.1002/star.201500071
dc.identifier.urihttps://hdl.handle.net/20.500.12514/1328
dc.identifier.volume68en_US
dc.identifier.wosWOS:000389311200025en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherWILEY-V C H VERLAG GMBHen_US
dc.relation.ispartofSTARCH-STARKEen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAnoxybacillus flavithermusen_US
dc.subjectalpha-Amylaseen_US
dc.subjectApple juice industryen_US
dc.subjectDetergent industryen_US
dc.subjectThermostableen_US
dc.titleProduction and characterization of thermostable alpha-amylase from thermophilic Anoxybacillus flavithermus sp nov SO-19en_US
dc.typeArticleen_US

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