Topic
Aldose
About: Aldose is a research topic. Over the lifetime, 1270 publications have been published within this topic receiving 27197 citations. The topic is also known as: aldoses.
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TL;DR: Condensation of 2,4-di-O -acetyl-3,6-di -O -methyl-α-d -glucopyranosyl bromide with either allyl or benzyl gave the title oligosaccharides in excellent yields.
18 citations
TL;DR: Simultaneous and sequential two‐step transformations by the phosphorylase–phosphatase combination catalyst yielded glycosyl phosphates of defined anomeric configuration in yields of up to 70 % based on the phosphate applied to the reaction.
Abstract: Sugar phosphates play an important role in metabolism and signaling, but also as constituents of macromolecular structures. Selective phosphorylation of sugars is chemically difficult, particularly at the anomeric center. We report phosphatase-catalyzed diastereoselective "anomeric" phosphorylation of various aldose substrates with α-D-glucose 1-phosphate, derived from phosphorylase-catalyzed conversion of sucrose and inorganic phosphate, as the phosphoryl donor. Simultaneous and sequential two-step transformations by the phosphorylase-phosphatase combination catalyst yielded glycosyl phosphates of defined anomeric configuration in yields of up to 70 % based on the phosphate applied to the reaction. An efficient enzyme-assisted purification of the glycosyl phosphate products from reaction mixtures was established.
18 citations
Patent•
20 Mar 1991
TL;DR: In this article, an enzymatic method is proposed for the preparation of a fructose-containing oligosaccharide, in which a.beta-fructofuranosidase obtained by culturing Arthrobacter sp. K-1 (FERM BP-3192) as an enzyme is reacted on sucrose, raffinose or stachyose as the donor in the presence of an aldose or ketose as a receptor.
Abstract: An enzymatic method is proposed for the preparation of a fructose-containing oligosaccharide, in which a .beta.-fructofuranosidase obtained by culturing Arthrobacter sp. K-1 (FERM BP-3192) as an enzyme is reacted on sucrose, raffinose or stachyose as the donor in the presence cf an aldose or ketose as the receptor. The enzyme is characterized by: (1) activity on sucrose for the transglycosidation of a fructosyl group to the receptor in the presence of a monosaccharide, sugar alcohol, alkyl alcohol, glycoside or oligosaccharide; (2) activity for the decomposition of sucrose, elrose, neokestose, xylsucrose, raf~inose and stachyose with inactivity on a saccharide selected from the group consisting of 1-kestose, nistose, inulobiose and levan biose; (3) optimum pH of 6.5 to 6.8 at 40°C with stability at a pH of 5.5 to 10; (4) optimum temperature of 55°C at a pH of 6.5 exhibiting at least 70% of residual activity at 60°C; (5) susceptibility to inhibition by the ions of silver, mercury, zinc, copper and tin; (6) two molecular weights of 52,000 ~ 2,500 and 58,000 ~ 2,500; and (7) two isoelectric points of pH 4.3 and pH 4.6.
18 citations
Patent•
18 May 2015
TL;DR: In this article, a continuous process for converting carbohydrates to ethylene and propylene glycol is described, where the carbohydrates are mixed with water and passed through a reactor at a temperature that hydrolyzes the carbohydrate mixture at least partially to monosaccharides.
Abstract: A continuous process for converting carbohydrates to ethylene and propylene glycol. The carbohydrates are mixed with water and passed through a reactor at a temperature that hydrolyzes the carbohydrate mixture at least partially to monosaccharides. The reactor has a first zone comprising a retro-aldol catalyst and a second zone comprising a reducing catalyst. The aldose is converted in the first zone into glycolaldehyde by the retro-aldol catalyst and the glycolaldehyde, in the presence of hydrogen, is converted to ethylene glycol in the second zone of the reactor. The reaction products are removed from the reactor and the ethylene glycol is recovered. The selectivity to propylene glycol can be enhanced via feeding ketose as the carbohydrate.
18 citations
TL;DR: Aldose reductase-catalyzed reduction of aldophosphamide appeared to be noncompetitively inhibited by sorbinil; the Ki value was 0.4 microM, and the in vivo significance of these observations is uncertain but could be of some magnitude since alcoph phosphamide is known to be only weakly cytotoxic.
18 citations