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KMID : 0613820110210020221
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Journal of Life Science
2011 Volume.21 No. 2 p.221 ~ p.226
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Enzymatic Characterization of a Thermostable 4-α-Glucanotransferase from Thermotoga neapolitana
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Choi Kyoung-Hwa
Seo Ja-Yeong
Kim Ji-Eun
Cha Jae-Ho
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Abstract
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The gene encoding 4--glucanotransferase (mgtA) from Thermotoga neapolitana was cloned and expressed in Escherichia coli in order to investigate whether this enzyme was capable of producing cycloamylose for industrial applications. MgtA was purified to homogeneity by HiTrap Q HP and Sephacryl S-200 HR column chromatographies. The size of the enzyme as determined by SDS-PAGE was about 52 kDa, which was in good agreement with its deduced molecular mass of 51.9 kDa. The optimal temperature and pH for the activity of the 4--glucanotransferase was found to be and 6.5, respectively. The enzyme hydrolyzed the 1,4--glucosidic bonds in oligomeric 1,4--glucans and transferred oligosaccharides (maltotriose being the shortest one) to acceptor maltodextrins. However, the enzymes had no activity against pullulan, glycogen, and other di- or trioligosaccharides with rare types of -bond. MgtA is distinguished from 4--glucanotransferase from Thermotoga maritima in that it can convert maltotriose into maltooligosaccharides. The treatment of glucoamylase after the reaction of MgtA with maltotriose, maltotetraose, maltopentaose, or maltohexaose as sole substrate revealed that MgtA yielded linear maltooligosaccharides instead of cycloamylose.
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KEYWORD
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4--Glucanotransferase, glycosyl hydrolase family 13, thermostability, Thermotoga neapolitana
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