Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Expression of Cyclomaltodextrinase Gene from Bacillus halodurans C-125 and Characterization of Its Multisubstrate Specificity

  • Kang, Hye-Jeong (Department of Food Science and Technology, Chungbuk National University) ;
  • Jeong, Chang-Ku (Department of Food Science and Technology, Chungbuk National University) ;
  • Jang, Myoung-Uoon (Department of Food Science and Technology, Chungbuk National University) ;
  • Choi, Seung-Ho (Department of Food Science and Technology, Chungbuk National University) ;
  • Kim, Min-Hong (MH2 Biochemical Co., Ltd.) ;
  • Ahn, Jun-Bae (Department of Food Service Industry, Seowon University) ;
  • Lee, Sang-Hwa (Department of Food and Nutrition, Seowon University) ;
  • Jo, Sook-Ja (Department of Food and Nutrition, Seowon University) ;
  • Kim, Tae-Jip (Department of Food Science and Technology, Chungbuk National University)
  • Published : 2009.06.30
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Abstract

A putative cyclomaltodextrinase (BHCD) gene was found from the genome of Bacillus halodurans C-125, which encodes 578 amino acids with a predicted molecular mass of 67,279 Da. It shares 42-59% of amino acid sequence identity with common cyclomaltodextrinase (CDase)-family enzymes. The corresponding gene was cloned by polymerase chain reaction (PCR) and the dimeric enzyme with C-terminal 6-histidines was successfully overproduced and purified from recombinant Escherichia coli. BHCD showed the highest activity against ${\beta}-CD$ at pH 7.0 and $50^{\circ}C$. Due to its versatile hydrolysis and transglycosylation activities, BHCD has been confirmed as a member of CDases. However, BHCD can be distinguished from other typical CDases on the basis of its novel multisubstrate specificity. While typical CDases have over 10 times higher activity on ${\beta}-CD$ than starch or pullulan, the CD-hydrolyzing activity of BHCD is only 2.3 times higher than pullulan. In particular, it showed significantly higher activity ratio of maltotriose to acarbose than other common CDase-family enzymes.

Keywords

References

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