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Chemistry, 18.11.2019 21:31 amelvin41

The enzyme glucose oxidase isolated from the mold penicillium notatum catalyzes the oxidation of β‑d‑glucose to d‑glucono‑δ‑lactone. this enzyme is highly specific for the β anomer of glucose and does not affect the α anomer. in spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose, that is, for solutions consisting of a mixture of β‑d‑glucose and α‑d‑glucose. what makes it possible for this test to measure total blood glucose? both α‑d‑glucose and β‑d‑glucose have a free anomeric carbon. the β anomer is present in a much higher concentration than the α anomer. both α‑d‑glucose and β‑d‑glucose are in the glucopyranose form. the rate of mutarotation between α‑d‑glucose and β‑d‑glucose is high. aside from increased sensitivity, what major advantage does glucose oxidase offer over fehling's reagent for measuring blood glucose? fehling's test cannot detect the presence of the β anomer. fehling's reagent is not specific to glucose, detecting other reducing sugars. fehling's test cannot be used in the lab to estimate the relative amount of glucose. fehling's reagent can only detect the linear form of glucose.

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