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- W1027553372 abstract "This chapter describes the assay method, purification procedure, and properties of mutarotase. When optical changes due to other reactions can be ruled out, standard polarimetric methods can be used to assay mutarotase. Anaerobic polarimetry to avoid the notatin reaction has been described. A chemical assay suitable for use in crude extracts is based on the more rapid oxidation of β- than α-glucose by buffered bromine solutions, alternatively, the β-glucose is oxidized with glucose oxidase, and the peroxide formed is assayed. These tested compounds are not substrates D-arabinose, L-xylose, 2-deoxy-D-glucose, 3-methyl-D-glucose, D-glucosamine, D-mannose, D-fructose, L-rhamnose. The following do not mutarotate spontaneously or in the presence of kidney mutarotase; sucrose, raffinose, mannitol, sorbitol. All the known mutarotase substrates contain a reducing pyranose ring in C1 conformation, with equatorial hydroxyls at C-2 and probably C-3. Mutarotase is inhibited by several glycosides and by equilibrium solutions of some sugars. The mold mutarotase shows an increase of activity up to pH 5.8, and the optimum may be even higher. The enzyme is stable at pH 9.1 for at least 20 minutes at 20°." @default.
- W1027553372 created "2016-06-24" @default.
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- W1027553372 date "1962-01-01" @default.
- W1027553372 modified "2023-09-24" @default.
- W1027553372 title "[24] Mutarotase" @default.
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- W1027553372 doi "https://doi.org/10.1016/s0076-6879(62)05208-8" @default.
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