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KMID : 0545120060160111809
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Journal of Microbiology and Biotechnology
2006 Volume.16 No. 11 p.1809 ~ p.1813
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Cloning and Overexpression of 4-α-Glucanotransferase from Thermus brockianus (TBGT) in E. coli
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Bang Bo-Young
Kim Han-Jo
Kim Hae-Yeong
Baik Moo-Yeol
Ahn Soon-Cheol
Kim Chung-Ho
Park Cheon-Seok
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Abstract
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A gene corresponding to 4--glucanotransferase () was cloned from the thermophilic bacterium Thermus brockianus. The nucleotide sequence analysis showed that the gene is composed of 1,503 nucleotides and encodes a polypeptide that is 500 amino acids long with a calculated molecular mass of 57,221 Da. The deduced amino acid sequences of Thermus brockianus (TBGT) exhibited a high level of similarity to the amino acid sequence of of Thermus thermophilus (86%), but low level of homology to that of E. coli (26%). The TBGT gene was overexpressed in E. coli BL21, and the corresponding recombinant enzyme was efficiently purified by Ni-NTA affinity chromatography. The enzymatic characteristics revealed that optimal pH and temperature were pH 6 and , respectively. Most interestingly, TBGT reacted with small oligosaccharides, especially maltotriose, to form various maltooligosaccharides by using its disproportionation activity.
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KEYWORD
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Amylomaltase, disproportionation, 4-α-glucanotransferase, Thermus brockianus, transglycosylation
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