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Asymmetric Reduction of Iminium Salt with Chiral Dihydropyridines
Authors:Naomichi Baba  Kazuyoshi Nishiyama  Jun’ichi Oda  Yuzo Inouye
Affiliation:Institute for Chemical Research, Kyoto University, Uji, Kyoto
Abstract:A gram positive bacterium (strain No. 109) isolated from soil as a producer of cyclodextrinase was identified as Bacillus coagulans. The cyclodextrinase from B. coagulans was purified to a homogeneous state by disc-electrophoresis after Streptomycin treatment, DEAE-Sephadex column chromatography, Ultrogel AcA44 gel filtration and hydroxyapatite column chromatography. The molecular weight of the enzyme was determined to be 6.2}104 by sodium dodecyl-sulfate gel electrophoresis. The isoelectric point of the enzyme was pH 5.0. The enzyme was most active at pH 6.2 and 50°C, and stable up to 45°C at pH 7.0 and in the range of pH 6.0 ~ 7.3 at 40°C on 2 hr incubation. This enzyme hydrolyzed linear maltooligosaccharides (such as maltotetraose (G4), maltopentaose (G5) and maltohexaose (G6)) and α-, β- and α-cyclodextrins (CDs) faster than maltotriose (G3) and short chain amylose ( /></span> 18), but did not hydrolyze maltose. The rates of hydrolysis for polysaccharides (such as starch, amylose and amylopectin) were below 1 % as compared to that for <i>β</i>-CD. The <i>Km</i> values for G3, G4, G5, G6, short chain amylose (<span class= /></span> 18) and α, <i>β</i>- and <i>γ</i>-CD were 4.5, 4.0,2.3,1.5,1.5,10,2.8 and 0.47 mM, respectively. The products with this enzyme had the α-configulation.</td>
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Keywords:Sal k 4  Salsola kali  profilin  cross-reactivity
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