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Esterase is an enzyme that catalyzes the hydrolysis of esters. It hydrolyzes esters of l-amino acids more rapidly than esters of D-amino acids. How can this enzyme be used to separate a racemic mixture of amino acids?
Solution
VerifiedEsterase can be used in a similar way that amynoacylase is used to separate a racemic mixture of amino acids. Aminoacylase is an enzyme that acts as a catalyst to L - N-acetyl-amino acids only. For esterase to work we would need to convert the amino acids in the mixture to their ester form since esterase catalyzes the hydrolysis of esters. To do this we can use SOCL and ethanol. Once the amino acids are in ester form, the esterase will increase the rate of hydrolysis of the esters of L-amino acids and not the D-amino acids. The leftover esters of D-amino acids can be separated and hydrolyzed with acid-catalysis to their amino acid forms. Separating compounds on the basis of different rates of reaction is called kinetic resolution.
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