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KMID : 1007520090180030776
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Food Science and Biotechnology
2009 Volume.18 No. 3 p.776 ~ p.781
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Expression of Cyclomaltodextrinase Gene from Bacillus halodurans C-125 and Characterization of Its Multisubstrate Specificity
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Kang Hye-Jeong
Jeong Chang-Ku
Jang Myoung-Uoon
Choi Seung-Ho
Kim Min-Hong
Ahn Jun-Bae
Lee Sang-Hwa
Jo Sook-Ja
Kim Tae-Jip
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Abstract
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putative cyclomaltodextrinase (BHCD) gene was found from the genome of Bacillus halodurans C-125, whichencodes 578 amino acids with a predicted molecular mass of 67,279 Da. It shares 42-59% of amino acid sequence identity withcommon 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 recombinantEscherichia coli. BHCD showed the highest activity against β-CD at pH 7.0 and 50oC. Due to its versatile hydrolysis andtransglycosylation activities, BHCD has been confirmed as a member of CDases. However, BHCD can be distinguished fromother typical CDases on the basis of its novel multisubstrate specificity. While typical CDases have over 10 times higher activityon β-CD than starch or pullulan, the CD-hydrolyzing activity of BHCD is only 2.3 times higher than pullulan. In particular, itshowed significantly higher activity ratio of maltotriose to acarbose than other common CDase-family enzymes.
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KEYWORD
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Bacillus halodurans C-125, cyclomaltodextrinase (CDase), gene cloning, enzymatic characterization, multisubstratespecificity
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