Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Molecular Cloning and Enzymatic Characterization of Cyclomaltodextrinase from Hyperthermophilic Archaeon Thermococcus sp. CL1

  • Lee, Jae-Eun (Graduate School of Biotechnology and Institute of Life Sciences and Resources, Kyung Hee University) ;
  • Kim, In-Hwan (Graduate School of Biotechnology and Institute of Life Sciences and Resources, Kyung Hee University) ;
  • Jung, Jong-Hyun (Graduate School of Biotechnology and Institute of Life Sciences and Resources, Kyung Hee University) ;
  • Seo, Dong-Ho (Graduate School of Biotechnology and Institute of Life Sciences and Resources, Kyung Hee University) ;
  • Kang, Sung-Gyun (Marine Biotechnology Research Center, Korea Ocean Research and Development Institute) ;
  • Holden, James F. (Department of Microbiology, University of Massachusetts) ;
  • Cha, Jaeho (Department of Microbiology, College of Natural Sciences, Pusan National University) ;
  • Park, Cheon-Seok (Graduate School of Biotechnology and Institute of Life Sciences and Resources, Kyung Hee University)
  • Received : 2013.03.04
  • Accepted : 2013.04.13
  • Published : 2013.08.28
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Abstract

Genome organization near cyclomaltodextrinases (CDases) was analyzed and compared for four different hyperthermophilic archaea: Thermococcus, Pyrococcus, Staphylothermus, and Thermofilum. A gene (CL1_0884) encoding a putative CDase from Thermococcus sp. CL1 (tccd) was cloned and expressed in Escherichia coli. TcCD was confirmed to be highly thermostable, with optimal activity at $85^{\circ}C$. The melting temperature of TcCD was determined to be $93^{\circ}C$ by both differential scanning calorimetry and differential scanning fluorimetry. A size-exclusion chromatography experiment showed that TcCD exists as a monomer. TcCD preferentially hydrolyzed ${\alpha}$-cyclodextrin (${\alpha}$-CD), and at the initial stage catalyzed a ring-opening reaction by cleaving one ${\alpha}$-1,4-glycosidic linkage of the CD ring to produce the corresponding single maltooligosaccharide. Furthermore, TcCD could hydrolyze branched CDs (G1-${\alpha}$-CD, G1-${\beta}$-CD, and G2-${\beta}$-CD) to yield significant amounts (45%, 40%, and 46%) of isomaltooligosaccharides (panose and $6^2$-${\alpha}$-maltosylmaltose) in addition to glucose and maltose. This enzyme is one of the most thermostable maltogenic amylases reported, and might be of potential value in the production of isomaltooligosaccharides in the food industry.

Keywords

References

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