585-88-6, Maltitol is a Tetrahydropyrans compound, ?involved in a variety of chemical synthesis. Rlated chemical reaction is continuously updated
585-88-6, It was tested whether the following saccharides could be used as substrates for alpha-isomaltosylglucosaccharide-forming enzyme. For the purpose, a solution of maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose, maltoheptaose, isomaltose, isomaltotriose, panose, isopanose, alpha,alpha-trehalose, kojibiose, nigerose, neotrehalose, cellobiose, gentibiose, maltitol, maltotriitol, lactose, sucrose, erlose, selaginose, maltosyl glucoside, or isomaltosyl glucoside was prepared. To each of the above solutions was added two units/g substrate of a purified specimen of alpha-isomaltosylglucosaccharide-forming enzyme from either Bacillus globisporus C9 strain obtained by the method in Experiment 4-2, or Bacillus globisporus C11 strain obtained by the method in Experiment 7-2, and the resulting solutions were adjusted to give a substrate concentration of 2% (w/v) and incubated at 30 C. and pH 6.0 for 24 hours. The enzyme solutions before and after the enzymatic reactions were respectively analyzed on TLC disclosed in Experiment 1 to confirm whether the enzymes act on these substrates. The results are in Table 11. TABLE 11 Enzymatic action Enzymatic action Enzyme of Enzyme of Enzyme of Enzyme of Substrate C9 strain C11 strain Substrate C9 strain C11 strain Maltose + + Nigerose + + Maltotriose ++ ++ Neotrehalose + + Maltotetraose +++ +++ Cellobiose – – Maltopentaose +++ +++ Gentibiose – – Maltohexaose +++ +++ Maltitol – – Maltoheptaose +++ +++ Maltotriitol + + Isomaltose – – Lactose – – Isomaltotriose – – Sucrose – – Panose – – Erlose + + Isopanose ++ ++ Selaginose – – alpha,alpha-Trehalose – – Maltosylglucoside ++ ++ Kojibiose + + Isomaltosylglucoside – – Note: Before and after the enzymatic reaction, the symbols ?-?, ?+?, ?++?, and ?+++? mean that it showed no change, it showed a slight reduction of the color of substrate spot and the formation of other reaction product, it showed a high reduction of the color of substrate No.spot and the formation of other reaction product, and it showed a substantial disappearance of the color of substrate spot and the formation of other reaction product, respectively. As evident from Table 11, it was revealed that the alpha-isomaltosylglucosaccharide-forming enzyme well acted on saccharides having a glucose polymerization degree of at least three and having a maltose structure at their non-reducing ends, among the saccharides tested. It was also found that the enzyme slightly acted on saccharides, having a glucose polymerization degree of two, such as maltose, kojibiose, nigerose, neotrehalose, maltotriitol, and erlose.
As the paragraph descriping shows that 585-88-6 is playing an increasingly important role.
Reference£º
Patent; Kubota, Michio; Nishimoto, Tomoyuki; Aga, Hajime; Fukuda, Shigeharu; Miyake, Toshio; US2006/8791; (2006); A1;,
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