Cloning, Expression, and Characterization of Bacillus sp. snu-7 Inulin Fructotransferase

A gene encoding inulin fructotransferase (di-D-fructofuranose 1,2':2,3' dianhydride [DFA Ⅲ]-producing IFTase, EC 4.2.2.18) from Bacillus sp. snu-7 was cloned. This gene was composed of a single, 1,353-bp open reading frame encoding a protein composed of a 40-amino acid signal peptide and a...

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Veröffentlicht in:	Journal of microbiology and biotechnology 2007-01, Vol.17 (1), p.37-43
Hauptverfasser:	Kim, C.S. (Seoul National University, Seoul, Republic of Korea), Hong, C.K. (Seoul National University, Seoul, Republic of Korea), Kim, K.Y. (Seoul National University, Seoul, Republic of Korea), Wang, Xiu Ling (Agricultural University of Hebei, Baoding, China), Kang, S.I. (Gwangju Institute of Science and Technology, Gwangju, Republic of Korea), E-mail: kangsu@gist.ac.kr, Kim, S.I. (Seoul National University, Seoul, Republic of Korea)
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus - enzymology Bacillus - genetics Bacillus sp. snu-7 Base Sequence Biological and medical sciences Biotechnology Cloning, Molecular difructofuranose anhydride DNA Primers - genetics DNA, Bacterial - genetics Enzyme Stability Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Expression Genes, Bacterial Hexosyltransferases - chemistry Hexosyltransferases - genetics Hexosyltransferases - metabolism Hydrogen-Ion Concentration Hydrolysis INULIN Inulin - metabolism inulin fructotransferase INULINA INULINE Molecular Sequence Data Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid Temperature
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Zusammenfassung:	A gene encoding inulin fructotransferase (di-D-fructofuranose 1,2':2,3' dianhydride [DFA Ⅲ]-producing IFTase, EC 4.2.2.18) from Bacillus sp. snu-7 was cloned. This gene was composed of a single, 1,353-bp open reading frame encoding a protein composed of a 40-amino acid signal peptide and a 410-amino acid mature protein. The deduced amino acid sequence was 98% identical to Arthrobacter globiformis C11-1 IFTase (DFA Ⅲ-producing). The enzyme was successfully expressed in E. coli as a functionally active, His-tagged protein, and it was purified in a single step using immobilized metal affinity chromatography.
ISSN:	1017-7825