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KMID : 0380620110430030369
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Korean Journal of Food Science and Technology
2011 Volume.43 No. 3 p.369 ~ p.374
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Molecular Cloning and Characterization of Maltogenic Amylase from Deinococcus geothermalis
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Jung Jin-Woo
Jung Jong-Hyun
Seo Dong-Ho
Kim Byung-Yong
Park Cheon-Seok
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Abstract
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A putative maltogenic amylase gene (DGMA) was cloned from the Deinococcus geothermalis DSM 11300 genome using the polymerase chain reaction. The gene encoded 608 amino acids with a predicted molecular mass of 68,704 Da. The recombinant DGMA was constitutively expressed using the pHCXHD plasmid. As expected, the recombinant DGMA hydrolyzed cyclodextrins and starch to maltose and pullulan to panose by cleaving the α-(1,4)- glycosidic linkages, as observed for typical maltogenic amylases. Characterization of the recombinant DGMA revealed that the highest maltogenic amylase activity occurred at 40oC and pH 6.0. The half-life of catalytic activity at 65oC and 55oC were 8.2 min and 187.4 min, respectively. DGMA mainly hydrolyzed β-cyclodextrin, soluble starch, and pullulan and its efficient ratio of those substrates was 9:4.5:1.
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KEYWORD
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maltogenic amylase, Deinococcus geothermalis, β-cyclodextrin, panose
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