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KMID : 0545120070170030454
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Journal of Microbiology and Biotechnology
2007 Volume.17 No. 3 p.454 ~ p.460
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Enzymatic Characterization and Substrate Specificity of Thermostable β-Glycosidase from Hyperthermophilic Archaea, Sulfolobus shibatae,Expressed in E. coli
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Park Na-Young
Cha Jae-Ho
Park Cheon-Seok
Kim Dae-Ok
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Abstract
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Enzymatic properties and substrate specificity of recombinant β-glycosidases from a hyperthermophilic archaeon, Sulfolobus shibatae (rSSG), were analyzed. rSSG showed its optimum temperature and pH at 95oC and pH 5.0, respectively. Thermal inactivation of rSSG showed that its half-life of enzymatic activity at 75oC was 15 h whereas it drastically decreased to 3.9 min at 95oC. The addition of 10 mM of MnCl2 enhanced the hydrolysis activity of rSSG up to 23% whereas most metal ions did not show any considerable effect. Dithiothreitol (DTT) and 2-mercaptoethanol exhibited significant influence on the increase of the hydrolysis activity of rSSG. rSSG apparently preferred laminaribiose (β1→3Glc), followed by sophorose (β1→2Glc), gentiobiose (β1→6Glc), and cellobiose (β1→4Glc). Various intermolecular transfer products were formed by rSSG in the lactose reaction, indicating that rSSG prefers lactose as a good acceptor as well as a donor. The strong intermolecular transglycosylation activity of rSSG can be applied in making functional oligosaccharides.
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KEYWORD
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β-Glycosidase, Sulfolobus shibatae, substrate specificity, transglycosylation reaction
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