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KMID : 0364820120480020156
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Korean Journal of Microbiology
2012 Volume.48 No. 2 p.156 ~ p.162
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Enzymatic Characterization of Salmonella typhimurium Mannitol Dehydrogenase Expressed in Escherichia coli
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Jang Myoung-Uoon
Park Jung-Mi
Kim Min-Jung
Kang Jung-Hyun
Lee So-Won
Kim Tae-Jip
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Abstract
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A mannitol dehydrogenase (StMDH) gene was cloned from Salmonella typhimurium LT2 (KCTC 2421) and
overexpressed in Escherichia coli. It has a 1,467 bp open reading frame encoding 488 amino acids with deduced
molecular mass of 54 kDa, which shares approximately 36% of amino acid identity with known long-chain
dehydrogenase/reductatse (LDR) family enzymes. The recombinant StMDH showed the highest activity at 30℃, and
pH 5.0 and 10.0 for D-fructose reduction and D-mannitol oxidation, respectively. On the contrary, it has no activity
on glucose, galactose, xylose, and arabinose. StMDH can catalyze the oxidative/reductive reactions between
D-fructose and D-mannitol only in the presence of NAD+
/NADH as coenzymes. These results indicate that StMDH is
a typical NAD+
/NADH-dependent mannitol dehydrogenase (E.C. 1.1.1.67).
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KEYWORD
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Salmonella typhimurium LT2, mannitol dehydrogenase, NAD+/NADH-dependent activity
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