Co-lyophilization with D-proline greatly enhances peroxidase's stereoselectivity in a non-aqueous medium.

The impact of co-lyophilizing horseradish peroxidase (HRP) with numerous amino acids and other chiral excipients on the enzyme's subsequent stereoselectivity [E(S/R)] in the sulfoxidation of thioanisole in 2-propanol was systematically investigated. While many improved the stereoselectivity of (and significantly activated) HRP, the greatest effect was observed with D-proline which enhanced the E(S/R) value by over an order of magnitude from synthetically meaningless to useful.