Enzyme electrodes sucrose

Matsumoto et al (41) prepared a multi-enzyme electrode using glucose oxidase, invertase, mutarotase, fructose-5-dehydrogenase, and catalase to simultaneously detect glucose, fructose, and sucrose in fruit juices and soft drinks. Detection of multi-components by enzyme sensors was also reported in analysis of sucrose and glucose in honey (42) and drinks (43), and L-malate and L-lactate in wines (44). 

E. Maestre, I. Katakis and E. Dominguez, Amperometric flow-injection determination of sucrose with a mediated tri-enzyme electrode based on sucrose phosphorylase and electrocatalytic oxidation of NADH, Biosens. Bioelectron., 16(1-2) (2001) 61-68. 

T. Hu, X.E. Zhang, Z.P. Zhang and L.Q. Chen, A screen-printed disposable enzyme electrode system for simultaneous determination of sucrose and glucose, Electroanalysis, 12 (2000) 868-870. 

Several other sensors are available that are based on the amperometric measurement of hydrogen peroxide produced by enzymatic reactions. The analytes measured include sucrose, lactose, ethanol, and L-lactate. A different enzyme is, of course, required for each species. In some cases, enzyme electrodes can be based on measuring oxygen or on measuring pH. 

Various research groups have developed enzyme electrodes for the determination of sucrose. The operational parameters of these sensors are listed in Table 10. 

Between 15 and 20 analyzers based on enzyme electrodes are on the market worldwide. They are one-parameter instruments for the measurement of glucose, galactose, uric add, choline, ethanol, lysine, lactate, pesti-ddes, sucrose, lactose, and the activity of a-amylase (Table 23). They provide for a negligible enzyme consumption of less than 1 pg per sample. 

Molasses is used as a main carbon source in many fermentations. Most of the carbohydrates such as glucose, fructose and sucrose in molasses can not be determined by spectro-photometric methods because test samples are not optically clear. Many reports on enzyme electrodes for these carbohydrates have been published (15,19,20,21). However, enzyme electrodes are not suitable for determination of these carbohydrates because enzymes are unstable and inhibitors of enzymes sometimes exist in a fermentation broth. 

Enzymatic methods Enzymatic methods are available for the analysis of bulk sweeteners in food and beverages enzyme electrodes and detection kits are available for several sweeteners (e.g., sucrose, glucose, etc.). The usage of enzyme methods is determined by conditions under which the enzyme is viable, i.e., heat, substrate concentration, water availability, and interferences. This methodology is a popular alternative to chromatographic methods due to its speed, portability, and wide range of application. 

Albery, J. W., Kaha, Y. N., and Magner, E. 1992. Amperometric enzyme electrodes. Part VI. Enzyme electrodes for sucrose and lactose. J. Electroanal. Chem. 325 83-93. 

Hamid JA, Moody GJ, Thomas JDR. Chemically immobilised tri-enzyme electrode for the determination of sucrose using fiow injection analysis. Analyst 1988 113 81. 

Satoh I., Karabe I. and Suzuki S. (1976) Enzyme electrode for sucrose. Biotech. Biceng., 18, 269-271. 

ATPase also catalyzed a passive Rb -Rb exchange, the rate of which was comparable to the rate of active Rb efflux. This suggested that the K-transporting step of H,K-ATPase is not severely limited by a K -occluded enzyme form, as was observed for Na,K-ATPase. Skrabanja et al. [164] also described the reconstitution of choleate solubilized H,K-ATPase into phosphatidylcholine-cholesterol liposomes. With the use of a pH electrode to measure the rate of H transport they observed not only an active transport, which is dependent on intravesicular K, but also a passive H exchange. This passive transport process, which exhibited a maximal rate of 5% of the active transport process, could be inhibited by vanadate and the specific inhibitor omeprazole, giving evidence that it is a function of gastric H,K-ATPase. The same authors demonstrated, by separation of non-incorporated H,K-ATPase from reconstituted H,K-ATPase on a sucrose gradient, that H,K-ATPase transports two protons and two ions per hydrolyzed ATP [112]. 

Yao T, Sato M, Kobayashi Y and Wasa T 1984 Row injection analysis for glucose by the combined use of an immobilized glucose oxidase reactor and a peroxidase electrode Ana/. Chim. Acta 165 291-6 Olsson B, Staibom E and Johansson G 1986 Determination of sucrose in the presence of glucose in a flow-injection system with immobilized multi-enzyme... 

Hydrolysis and other Reactions and Features.—A. novel method for following the add catafysed hydrolysis of sucrose and lactose involves measurement of the rate of reaction of periodate with quenched aliquot portions of the solutions using a periodate>sensitive electrode. In this way sucrose could be determined in the presence of other carbohydrates in the range 0.01-0.1 M, and the method was applied to food products. The glycosidic hydrolysis of fluorenone ketal (107), which serves as a nucleoside glycosylase enzyme model, has been shown to be intramolecularly catalysed by comparison with analogous compounds. ... 

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