Characterization of Cyclodextrin Glucanotransferase Produced by <Emphasis Type="Italic">Bacillus megaterium</Emphasis> |
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Authors: | Ivan Pishtiyski Viara Popova Boriana Zhekova |
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Institution: | (1) Department of Biochemistry and Molecular Biology, University of Food Technologies, 26 Maritza Blvd., 4000 Plovdiv, Bulgaria |
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Abstract: | Cyclodextrin glucanotransferase, produced by Bacillus megaterium, was characterized, and the biochemical properties of the purified enzyme were determined. The substrate specificity of the
enzyme was tested with different α-1,4-glucans. Cyclodextrin glucanotransferase displayed maximum activity in the case of
soluble starch, with a K
m value of 3.4 g/L. The optimal pH and temperature values for the cyclization reaction were 7.2 and 60 °C, respectively. The
enzyme was stable at pH 6.0–10.5 and 30 °C. The enzyme activity was activated by Sr2+, Mg2+, Co2+, Mn2+, and Cu2+, and it was inhibited by Zn2+and Ag+. The molecular mass of cyclodextrin glucanotransferase was established to be 73,400 Da by sodium dodecyl sulfate–polyacrylamide
gel electrophoresis, 68,200 Da by gel chromatography, and 75,000 Da by mass spectrometry. The monomer form of the enzyme was
confirmed by the analysis of the N-terminal amino acid sequence. Cyclodextrin glucanotransferase formed all three types of
cyclodextrins, but the predominant product was β-cyclodextrin. |
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Keywords: | Cyclodextrin glucanotransferase Cyclodextrins Enzyme characterization Bacillus megaterium Application |
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