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.
Yu
Ju-Hyun
JH
Department of Chemistry and Division of Biological Engineering, Massachusetts Institute of Technology, Cambridge, 02139, USA.
Klibanov
Alexander M
AM
D019840:2-Propanol / Q000737:chemistry*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D005612:Freeze Drying / Q000379:methods; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011392:Proline / Q000737:chemistry*; D012451:Safrole / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D013237:Stereoisomerism; D013440:Sulfides / Q000737:chemistry / Q000378:metabolism
D013440:Sulfides; D011392:Proline; C093850:methylphenylsulfide; D006735:Horseradish Peroxidase; D019840:2-Propanol; D012451:Safrole; C005746:sulfoxide