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KMID : 0364820170530030208
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Korean Journal of Microbiology
2017 Volume.53 No. 3 p.208 ~ p.215
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Functional expression and enzymatic characterization of cyclomaltodextrinase from Streptococcus pyogen
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Jang Myoung-Uoon
Kang Hye-Jeong
Jung Chang-Ku
Oh Gyu-Won
Lee Eun-Hee
Son Byung-Sam
Kim Tae-Jip
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Abstract
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A cyclomaltodextrinase (SPCD) gene was cloned from Streptococcus pyogenes ATCC 700294. Its open reading frame
consists of 567 amino acids (66.8 kDa), which shows less than 37% of amino acid sequence identity with the other CDasefamily enzymes. The homo-dimeric SPCD with C-terminal six-histidines was expressed and purified from Escherichia coli. It showed the highest activity at pH 7.5 and 45°C, respectively. SPCD has the broad substrate specificities against β-cyclodextrin, starch, and maltotriose to produce mainly maltose, whereas it hydrolyzes pullulan to panose. It can also catalyze the hydrolysis of acarbose to glucose and acarviosineglucose. Interestingly, it showed much higher activity on β -cyclodextrin and acarbose than that on starch, pullulan, or maltotriose, which makes SPCD distinguished from common CDase-family enzymes. Although SPCD has significantly high acarbose-hydrolyzing activity, it showed negligible transglycosylation activity.
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KEYWORD
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Streptococcus pyogenes, cyclomaltodextrinase (CDase), enzymatic characterization, gene expression
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