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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20 citations
TL;DR: On fait reagir ici le triphenylsilane dans des conditions radicalaires sur divers furanoses and pyranoses as mentioned in this paper, a.k.a.
Abstract: On fait reagir ici le triphenylsilane dans des conditions radicalaires sur divers furanoses et pyranoses
20 citations
TL;DR: Peracetylated α-glycopyranosyl fluorides of di- and tri-saccharides were obtained in good yields by treatment of the corresponding peracetyl-ated di-and tri-scharides with pyridinium poly(hydrogen fluoride) as mentioned in this paper.
20 citations
TL;DR: In this article, a series of sulfated complex metal oxides were synthesized for the conversion of aldose-based mono-, di-, and poly-saccharides, as well as starchy food waste into EMF.
20 citations
TL;DR: Niederpruem and Doudoroff as mentioned in this paper showed that aldoses require an unidentified cofactor which is present in the particulate fraction of aerobic cells, but is unavailable to the enzyme system.
Abstract: Niederpruem, Donald J (University of California, Berkeley), and Michael Doudoroff Cofactor-dependent aldose dehydrogenase of Rhodopseudomonas spheroides J Bacteriol 89: 697–705 1965—Particulate enzyme preparations of cell extracts of Rhodopseudomonas spheroides possess constitutive dehydrogenase and oxidase activities for aldose sugars, reduced nicotinamide adenine dinucleotide (NADH 2 ), and succinate The dehydrogenation of aldoses requires an unidentified cofactor which is not required for the oxidation of succinate nor of NADH 2 The cofactor is present in the particulate fraction of aerobic cells, but is unavailable to the enzyme system It can be liberated by boiling or by treatment with salts at high concentration The cofactor also appears in the soluble fraction of aerobic cells, but only after exponential growth has ceased Extracts of cells grown anaerobically in the light possess the apoenzyme, but not the cofactor, for aldose oxidation Cofactor activity was found in extracts of Bacterium anitratum (= Moraxella sp) but not in Escherichia coli, Pseudomonas fluorescens , yeast, or mouse liver In 0075 m tris(hydroxymethyl)aminomethane-phosphoric acid buffer ( p H 73), the oxidation of NADH 2 was stimulated and succinoxidase was inhibited by high salt concentrations
19 citations