A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties

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Veröffentlicht in:	International journal of molecular sciences 13(2012), 8, Seite 10505-10522
Personen und Körperschaften:	Ibrahim, Abdelnasser S. S. (VerfasserIn), Al-Salamah, Ali A. (VerfasserIn), El-Tayeb, Mohamed A. (VerfasserIn), Elbadawi, Yahya B. (VerfasserIn), Antranikian, Garabed (VerfasserIn), Technische Universität Hamburg (Sonstige, Sonstige Körperschaft), Technische Universität Hamburg Institut für Technische Mikrobiologie (Sonstige, Sonstige Körperschaft)
Titel:	A novel cyclodextrin glycosyltransferase from alkaliphilic amphibacillus sp. NPST-10: purification and properties/ Abdelnasser S. S. Ibrahim, Ali A. Al-Salamah, Mohamed A. El-Tayeb, Yahya B. El-Badawi and Garabed Antranikian
Format:	E-Book-Kapitel
Sprache:	Englisch
veröffentlicht:	2012
Gesamtaufnahme:	: International journal of molecular sciences, 13(2012), 8, Seite 10505-10522 , volume:13
Quelle:	Verbunddaten SWB Lizenzfreie Online-Ressourcen

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Zusammenfassung:	Screening 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 identified the isolate as Amphibacillus. 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 −1 protein, 20.0 U mg protein and 11.0 U mg 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 and 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, and 2-mercaptoethanol. To the best of our knowledge, this is the first report of CGTase production by Amphibacillus. The achieved high conversion of insoluble raw corn starch into cyclodextrins (67.2%) with production of mainly β-CD (86.4%), makes Amphibacillus NPST-10 desirable for the cyclodextrin production industry.
Umfang:	Illustrationen
ISSN:	1422-0067
DOI:	10.3390%2Fijms130810505