Properties of Sorbitol Dehydrogenase from Pseudomonas sp. KS-E1806 and Comparison with Other Sorbitol Dehydrogenases
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概要
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Sorbitol dehydrogenase (SDH, EC 1.1.1.14) was purified to homogeneity from a cell-free extract of Pseudomonas sp. KS-E1806 by chromatographies with QAE-Sephadex A-50,QAE-Toyopearl 550C, and Bio-Gel A-1.5m. The molecular weight of the enzyme was estimated to be 64,500 and 27,400 by gel filtration and SDS-PAGE, respectively, suggesting that it has a dimeric structure. The enzyme was stable from pH 5.5 to 10.5,and below 40℃ for 30 min at pH 9.0 D-Sorbitol and galactitol were good substrates of the enzyme, whereas it acted only slightly on xylitol and D-mannitol. The enzyme was superior to sheep liver SDH with respect to substrate specificity and pH stability, and it was more thermostable than a previously reported Pseudomonas sp. SDH. Compared with other known SDHs, the enzyme from Pseudomonas sp. KS-E1806 has several advantages for practical use in the enzymatic analysis of D-sorbitol.
- 公益社団法人日本生物工学会の論文
- 1997-09-25
著者
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Minamihara Tomoyuki
Research & Development Division Kikkoman Corporation
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Suzuki Masaru
Research & Development Division Kikkoman Corporation
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