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dc.contributor.authorIbrahim, Abdelnasser S. S.-
dc.contributor.authorAl-Salamah, Ali A.-
dc.contributor.authorEl-Tayeb, Mohamed A.-
dc.contributor.authorElbadawi, Yahya B.-
dc.contributor.authorAntranikian, Garabed-
dc.date.accessioned2017-08-29T10:23:34Z-
dc.date.available2017-08-29T10:23:34Z-
dc.date.issued2012-08-22-
dc.identifierdoi: 10.3390/ijms130810505-
dc.identifier.citationInternational Journal of Molecular Sciences 13 (2012), 8, S. 10505-10522de
dc.identifier.issn1422-0067de
dc.identifier.urihttp://tubdok.tub.tuhh.de/handle/11420/1423-
dc.description.abstractScreening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis<strong> </strong>identified the isolate as <em>Amphibacillus</em><em> </em>sp. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg<sup>−1</sup> protein, 20.0 U mg<sup>−1</sup> protein and 11.0 U mg<sup>−1</sup> protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl<sub>2</sub>. <em>K</em><sub>m</sub> and <em>V</em><sub>max</sub> values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co<sup>2+</sup>, Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup>, Ba<sup>2+</sup>, Cd<sup>2+</sup>, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by <em>Amphibacillus</em> sp. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes <em>Amphibacillus</em> sp. NPST-10 desirable for the cyclodextrin production industry.-
dc.description.abstractScreening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis<strong> </strong>identified the isolate as <em>Amphibacillus</em><em> </em>sp. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg<sup>−1</sup> protein, 20.0 U mg<sup>−1</sup> protein and 11.0 U mg<sup>−1</sup> protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl<sub>2</sub>. <em>K</em><sub>m</sub> and <em>V</em><sub>max</sub> values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co<sup>2+</sup>, Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup>, Ba<sup>2+</sup>, Cd<sup>2+</sup>, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by <em>Amphibacillus</em> sp. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes <em>Amphibacillus</em> sp. NPST-10 desirable for the cyclodextrin production industry.en
dc.publisherMultidisciplinary Digital Publishing Institutede
dc.relation.ispartofInternational Journal of Molecular Sciencesde
dc.rightsCC BY 3.0de
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.subject.ddc570: Biowissenschaften, Biologiede
dc.titleA novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10 : purification and propertiesde
dc.typeArticlede
dc.date.updated2017-08-24T09:55:01Z-
dc.identifier.urnurn:nbn:de:gbv:830-882w02166-
dc.identifier.doi10.15480/882.1420-
dc.type.diniarticle-
dc.subject.ddccode570-
dcterms.DCMITypeText-
tuhh.identifier.urnurn:nbn:de:gbv:830-882w02166de
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tuhh.gvk.ppn89678701X-
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dc.identifier.hdl11420/1423-
tuhh.abstract.englishScreening for cyclodextrin glycosyltransferase (CGTase)-producing alkaliphilic bacteria from samples collected from hyper saline soda lakes (Wadi Natrun Valley, Egypt), resulted in isolation of potent CGTase producing alkaliphilic bacterium, termed NPST-10. 16S rDNA sequence analysis<strong> </strong>identified the isolate as <em>Amphibacillus</em><em> </em>sp. CGTase was purified to homogeneity up to 22.1 fold by starch adsorption and anion exchange chromatography with a yield of 44.7%. The purified enzyme was a monomeric protein with an estimated molecular weight of 92 kDa using SDS-PAGE. Catalytic activities of the enzyme were found to be 88.8 U mg<sup>−1</sup> protein, 20.0 U mg<sup>−1</sup> protein and 11.0 U mg<sup>−1</sup> protein for cyclization, coupling and hydrolytic activities, respectively. The enzyme was stable over a wide pH range from pH 5.0 to 11.0, with a maximal activity at pH 8.0. CGTase exhibited activity over a wide temperature range from 45 °C to 70 °C, with maximal activity at 50 °C and was stable at 30 °C to 55 °C for at least 1 h. Thermal stability of the purified enzyme could be significantly improved in the presence of CaCl<sub>2</sub>. <em>K</em><sub>m</sub> and <em>V</em><sub>max</sub> values were estimated using soluble starch as a substrate to be 1.7 ± 0.15 mg/mL and 100 ± 2.0 μmol/min, respectively. CGTase was significantly inhibited in the presence of Co<sup>2+</sup>, Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup>, Ba<sup>2+</sup>, Cd<sup>2+</sup>, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by <em>Amphibacillus</em> sp. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes <em>Amphibacillus</em> sp. NPST-10 desirable for the cyclodextrin production industry.de
tuhh.relation.ispartofInternational Journal of Molecular Sciencesde
tuhh.publisher.doi10.3390/ijms130810505-
tuhh.publication.instituteTechnische Mikrobiologie V-7de
tuhh.identifier.doi10.15480/882.1420-
tuhh.type.opus(wissenschaftlicher) Artikelde
tuhh.institute.germanTechnische Mikrobiologie V-7de
tuhh.gvk.hasppnfalse-
tuhh.hasurnfalse-
openaire.rightsinfo:eu-repo/semantics/openAccessde
dc.type.driverarticle-
dc.rights.ccbyde
dc.rights.ccversion3.0de
dc.type.casraiJournal Articleen
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