Cloning and Expression of the 4-α-Glucanotransferase Gene from the Hyperthermophilic Archaeon Pyrococcus sp. KOD1,and Characterization of the Enzyme

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概要

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• The 4-α-glucanotransferase gene (gtpK) of a hyperthermophilic archaeon Pyrococcus sp. KOD1 was cloned and the nucleotide sequence analysis showed that the gtpK gene is composed of 1,973 bp, which encodes a protein of 653 amino acids with a calculated molecular weight of 76,693 Da. The gtpK was then overexpressed under the control of the lac promoter in Escherichia coli. The enzyme was purified by heat treatment, hydrophobic interaction chromatography, and anion-exchange chromatography. GtpK could react each maltooligosaccharides (from maltose to maltoheptaose) as the effective substrate to form glucose and various maltooligosaccharides containing higher polymeric molecules than the substrate. These results showed that GtpK is a 4-α-glucanotransferase which transfers the glucosyl and maltooligosyl units to a new C-4 position in another maltooligosaccharides and glucose. The optimum temperature and pH for the enzyme activity were found to be 100℃ and 6-8,respectively, and the enzyme was considerably stable even after heating at 100℃ for 30 min. When the deduced amino acid sequence of GtpK was compared with the protein sequences available in the databases, only two significant similar enzymes (α-amylases of Pyrococcus furiosus and Dictyoglomus thermophilum exhibited an identity of 68.3% and 36.0%, respectively) were found. Interestingly, only these three homologous enzymes did not preserve the conserved regions of α-amylase family, but the other α-amylases and 4-α-glucanotransferase are classified into the α-amylase family since all enzymes have the conserved homologous regions. Therefore, we consider that these enzymes, including GtpK, are classified into a new family of starch-degrading enzymes.

• 社団法人日本生物工学会の論文
• 1997-06-25

著者

• Takagi Masahiro

  School Of Materials Science Japan Advanced Institute Of Science And Technology

• Takagi M

  School Of Materials Science Japan Advanced Institute Of Science And Technology

• FUJIWARA SHINSUKE

  Department of Bioscience, School of Science and Technology, Kwansei Gakuin University

• IMANAKA Tadayuki

  Department of Synthetic and Biological Chemistry, Graduate School of Engineering, Kyoto University

• TAKAGI MASAHIRO

  Department of Biotechnology, Graduate School of Engineering, Osaka University

• TACHIBANA YOSHIHISA

  Research and Development Center, Nagase Co.Ltd.

• Fujiwara S

  School Of Science And Engineering Department Of Life Science Kwansei-gakuin University

• Fujiwara Shinsuke

  Department Of Biotechnology Graduate School Of Engineering Osaka University

• Fujiwara Shinsuke

  Department Of Bioscience School Of Science And Technology Kwansei Gakuin University

• TACHIBANA YOSHIHISA

  Nagase Biochemicals Ltd.

• Takagi M

  Nagasaki Univ. Nagasaki Jpn

• Imanaka Tadayuki

  Department Of Applied Biotechnology Faculty Of Engineering Osaka University

• Fujiwara Shinsuke

  School Of Science And Engineering Department Of Life Science Kwansei-gakuin University

• Tachibana Yoshihisa

  Research And Development Center Nagase Co.ltd.

• Takagi Masahiro

  Department Of Biotechnology Faculty Of Engineering Osaka University

• Fujiwara Shinsuke

  Department Of Bioscience Graduate School Of Science And Technology Kwansei-gakuin University:researc

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