Hye-Jeong Kang, Chang-Ku Jeong, Myoung-Uoon Jang, Seung-Ho Choi, Tae-Jip Kim, Min-Hong Kim, Jun-Bae Ahn, Sang-Hwa Lee, Sook-Ja Jo
언어
영어(ENG)
URL
https://www.earticle.net/Article/A108266
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원문정보
초록
영어
A 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.
목차
Abstract Introduction Materials and Methods Results and Discussion References