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?
Answer 1a) The α anomer of glucose easily converts to the β anomer.
Reason- There is a very high rate of mutarotation between α anomer and β anomer. it means that α and β anomers can be easily interconverted. when β anomer of glucose is consumed by the enzyme glucose oxidase, α anomer gets converted to β anomer. in this way, total blood glucose level can be measured by the enzyme glucose oxidase.
Answer 2c) Fehling's reagent is not specific to glucose, detecting other reducing sugars.
Reason- Fehling reagent can react with any reducing sugar, while enzyme glucose oxidase specifically reacts with the glucose molecules. that is why glucose oxidase provides another advantage over Fehling's reagent.
The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-D-glucose to...