Final answer:
The enzyme in question is specific to the alpha anomer and will only catalyze reactions with substrates that match its active site's specific shape and stereochemistry, leaving the beta anomers unaltered.
Step-by-step explanation:
An enzyme that specifically recognizes only the alpha anomer as a substrate and converts it to a product will not directly interact with the beta anomer in a mixture. The enzyme binds to substrates at its active site, which has a unique shape that determines the specificity for the substrate. If the -OH group on the anomeric carbon atom is towards the right, it is known as the alpha (a) anomer, and if towards the left, it is the beta (B) anomer.
The enzyme's active site is transformed in the presence of its correct substrate through an "induced fit" process to achieve an optimal binding and catalysis of the reaction. However, if the enzyme is chiral, similar to most biological enzymes, it will typically produce one enantiomer exclusively. In this case, alpha anomers will be converted to products, and due to the enzyme's chiral nature and specificity, beta anomers will not be converted unless they undergo a transformation that makes them suitable for the enzyme's active site.
Stereospecific reactions in enzymes are a result of this kind of specificity, as enzymes are proteins composed of amino acids in the L-configuration, leading to a chiral binding site that favors interactions with substrates of a specific stereochemistry. Consequently, this enzyme's ability to process substrates will be limited to those molecules that match its active site's stereochemistry.