著者

Hiromichi Itoh Hiroaki Okaya Anisur Rahman Khan Shigeyuki Tajima Shigeru Hayakawa Ken Izumori

出版者

(社)日本農芸化学会

雑誌

Bioscience, Biotechnology, and Biochemistry (ISSN:09168451)

巻号頁・発行日

vol.58, no.12, pp.2168-2171, 1994-12-23 (Released:2008-02-08)

参考文献数

11

被引用文献数

41 137

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A new enzyme, D-tagatose 3-epimerase, was found in Pseudomonas sp. ST-24 during the course of studies on D-sorbose fermentation. This new enzyme catalyzes epimerization of keto-sugars, for example between D-tagatose and D-sorbose, and between D-fructose and D-psicose. It was shown that this enzyme epimerizes the configuration at the C-3 position of these substrates. This epimerase didn't act on D-fructose 6-phosphate and D-ribulose 5-phosphate. The enzyme has been purified from cells grown on a medium containing 1% D-glucose and 0.05% D-tagatose, and it appeared homogeneous on electrophoresis. The enzyme has a molecular weight of about 68, 000 by gel filtration and consists of two subunits identical in molecular weight (about 33, 000 by SDS-PAGE). The maximum activity at 30°C was obtained at pH 7-9, and the enzyme was stable from pH 7-11. The optimum temperature was around 60°C, and it was stable up to 60°C for 10 min.