In: Biology
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.