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Title 

Molecular cloning and characterization of trehalose synthase from Thermotoga maritima DSM3109: Syntheses of trehalose disaccharide analogues and NDP-glucoses

Authors 

S I RyuJ E KimN T HuongEui-jeon WooS K MoonS B Lee

Publisher 

Elsevier

Issue Date 

2010

Citation 

Enzyme and Microbial Technology, vol. 47, no. 6, pp. 249-256

Keywords 

Disaccharide analogueHyperthermophileNucleoside diphosphate-glucoseThermotoga maritimaTrehaloseTrehalose synthase

Abstract 

A gene (ORF TM0392) encoding a putative trehalose synthase (TmTreT) in Thermotoga maritima was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity by heat treatment and a glutathione-sepharose affinity column chromatography. The purified enzyme existed exclusively as a monomer in a native state. The optimum pH and temperature for this enzyme were 6.0 and 65°C. The glutathione-S-transferase (GST)-fusion enzyme had greater thermostability than thrombin-treated free enzyme. TmTreT had diverse substrate specificities. The enzyme effectively created a free trehalose from several nucleoside diphosphate (NDP)-glucoses as a donor and glucose as an acceptor. Inversely, the enzyme was also capable of employing several NDPs such as UDP, ADP, GDP, and CDP with trehalose to produce corresponding NDP-glucoses. The enzyme was able to employ other monosaccharides, such as mannose and fructose, as acceptors to synthesize disaccharide analogues of trehalose. The mannose-containing analogue was not hydrolyzed by trehalase and the rat intestinal enzymes. Furthermore, the analogue showed a competitive inhibition to the intestinal disaccharidases with Ki values of approximately 0.8-1.6mM. The results suggest that the enzyme is an useful trehalose synthase that can regenerate NDP-glucoses from NDPs and produce the inhibitory trehalose analogues of indigestible disaccharides.

ISSN 

0141-0229

Link 

http://dx.doi.org/10.1016/j.enzmictec.2010.07.017

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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