Cyclodextrin production by Bacillus lehensis isolated from cassava starch: Characterisation of a novel enzyme

The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of sub...

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Veröffentlicht in:Czech Journal of Food Sciences 2014-01, Vol.32 (1), p.48-53
Hauptverfasser: Blanco, K.C., University Estadual Paulista, Rio Claro (Brazil). Dept. of Biochemistry and Microbiology, De Moraes, F.F., University Estadual de Maringa (Brazil). Chemical Engineering Dept, Bernardi, N.S., University Estadual Paulista, Rio Claro (Brazil). Dept. of Biochemistry and Microbiology, Vettori, M.H.P.B., University Estadual Paulista, Rio Claro (Brazil). Dept. of Biochemistry and Microbiology, Monti, R., University Estadual Paulista, Rio Claro (Brazil). Dept. of Biochemistry and Microbiology, Contiero, J., University Estadual Paulista, Rio Claro (Brazil). Dept. of Biochemistry and Microbiology
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Sprache:eng
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Zusammenfassung:The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cyclodextrin glycosyltransferase were 55 deg C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l/h.
ISSN:1212-1800
1805-9317
DOI:10.17221/432/2012-CJFS