Zur enzymatischen Bestimmung von Glucose und Fructose in Wein

Möhler, Klement; Looser, Siegfried

doi:10.1007/bf01786893

Cited by 3 publications

(1 citation statement)

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“…Joergensen and Joergensen (135) used glucose oxidase to determine which glucose anomer was produced in the 0-glucosidase degradation of maltose, and Rohwer, Henschel, and Engel (262) assayed glucose in starch hydrolysates, corn syrups, and sugar solutions. Moehler and Looser (195) determined glucose and fructose in urine and Weichel proposed enzymic methods for the assay of fructose (347). White measured glucose in honey by a photometric procedure in which contaminant invertase was inhibited by tris buffer (350), and Tengstrom (328) determined both glucose and galactose in urine.…”

Section: Determination Of Substratesmentioning

confidence: 99%

Use of enzymes in analytical chemistry

Guilbault¹

1968

Anal. Chem.

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Both of these contain valuable procedures for enzyme analysis. Guilbault (97) has authored a chapter on fluorometric methods of analysis of enzymes, substrates, activators, and inhibitors in his book, "Fluorescence. Theory, Instrumentation and Practice." Passwater's book,(233) "Guide to the Umbelliferone (7 -hydroxy coumarin) and 4-methyl-umbelliferone are highly fluorescent compounds which have been modified to form nonfluorescent substrates for the enzymes glucuronidase, glucosidase, Ar-acetyl-/3-glucosaminidase, and ß-galactosidase. Robinson (259) used 4-methylumbelliferone^-Dglucoside as a substrate for ß-glucosidase. The substrate is split specifically by this enzyme, thus permitting the separate identification of ß-glucosidase and ß-glucuronidase in paper electrophoresis. Woolen and Turner (358, 359) assayed ß-glucuronidase in plasma using 4-methyl umbelliferylß-glucuronide as substrate, and Woolen and Walker (360), proposed 4-methyl umbelliferone-.Y-acetyl -ß-D-glucosaminide and 4-methyl umbelliferone-ß-D-galactoside as substrates for V-acetylß-D-glucosaminidase and ß-galactosidase. Likewise, Leaback (169) described conditions for the continuous fluorometric assay of Y-acetyl^-Dglucosaminidase using the same substrate, and Veritz, Gambell, and Brown (336) proposed l-naphthyl-2-acetamido-2-deox3T^-D-glucop3"ranoside as a substrate for this enzyme. The production of 1-naphthol was proportional to the concentration of enzyme.Greenberg (96) assayed ß-glucuroni-

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Section: Determination Of Substratesmentioning

confidence: 99%