Enzymatic determination of glucose in culture liquor with glucose oxidase for use in food

1985 ◽  
Vol 19 (3) ◽  
pp. 216-219 ◽  
Author(s):  
A. N. Khalyutkin ◽  
E. I. Prokopenko ◽  
S. B. Itsygin ◽  
O. V. Karpova ◽  
T. A. Kovaleva ◽  
...  
1965 ◽  
Vol 11 (9) ◽  
pp. 840-845 ◽  
Author(s):  
Michael Robin ◽  
Abraham Saifer

Abstract An automated procedure for the enzymatic determination of "true" glucose with the glucose oxidase-peroxidase system is described. A threefold increase in sensitivity was obtained through measurement of the stable, pink chromogen obtained at high acid concentration. Good reproducibility and stoichiometry was obtained over the range of 50-400 mg./l00 ml. at a sampling rate of 40/hr. The normal range (70-105 mg./100 ml.) and the error of the method (±2.0%) are about the same as that obtained with the manual method of Saifer and Gerstenfeld (7).


1969 ◽  
Vol 52 (5) ◽  
pp. 956-958
Author(s):  
W W Turner

Abstract Starch is determined in various materials such as feeds, grains, cereals, grasses, and feces by the combination of some existing techniques plus new methodology. Samples are extracted with aqueous alcohol and hydrolyzed with HCl; the resulting glucose is measured with a glucose oxidase enzyme system. The actual handling operations, including troublesome nitrations and constant temperature baths, are minimized or eliminated.


1998 ◽  
Vol 368 (1-2) ◽  
pp. 97-104 ◽  
Author(s):  
Jose F Sierra ◽  
Javier Galban ◽  
S de Marcos ◽  
Juan R Castillo

1984 ◽  
Vol 30 (2) ◽  
pp. 293-294 ◽  
Author(s):  
K Soyama

Abstract A new and simple enzymatic assay for measuring D-mannose in serum is described. Endogenous glucose is eliminated from serum by use of glucose oxidase (EC 1.1.3.4) and catalase (EC 1.11.1.6). D-Mannose concentration is calculated from the increase in NADH formation after mannosephosphate isomerase (EC 5.3.1.8) is added. This increase is a result of coupling the following series of enzymes: hexokinase (EC 2.7.1.1), glucosephosphate isomerase (EC 5.3.1.9), and glucose-6-phosphate dehydrogenase (EC 1.1.1.49, NAD+-dependent). The study included subjects who were healthy volunteers and patients with suspected or proven fungal infections.


Diabetes ◽  
1956 ◽  
Vol 5 (1) ◽  
pp. 1-6 ◽  
Author(s):  
E. R. Froesch ◽  
A. E. Renold ◽  
B. McWilliams

1961 ◽  
Vol 7 (5) ◽  
pp. 542-545 ◽  
Author(s):  
Mary E Washko ◽  
Eugene W Rice

Abstract The glucose oxidase-peroxidase system for the enzymatic determination of glucose was investigated with respect to the instability of the enzyme reagent, the buffering capacity of the reaction milieu, and the stability and sensitivity of the final chromogen. An improved procedure was developed in which the enzyme solution is both stabilized and more adequately buffered by reconstitution in 40% aqueous glycerol containing 0.04 M phosphate buffer, pH 7.0. The sensitivity and stability of the colored product is markedly increased when a final sulfuric acid concentration of 4.9 N is used.


1963 ◽  
Vol 41 (5) ◽  
pp. 265-268 ◽  
Author(s):  
Thomas J Cook ◽  
Allan L Lorincz ◽  
Alan R Spector

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