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 clinical assay for total blood glucose (α and β forms). how is this possible? aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over fehling’s reagent for the determination of blood glucose?