Mechanism of activation of subtilisn Carlsberg in organic solvents by co-lyophilization with methyl α-cyclodextrin

ORGN 386

Ezio Fasoli, fasoli@quimica.uprh.edu1, Betzaida Castillo2, Eduardo Rosario, dream_knight80@hotmail.com1, Vibha Bansal, vbansal@quimica.uprh.edu1, Amaris Ferrer1, and Gabriel L. Barletta, barletta@quimica.uprh.edu1. (1) Department of Chemistry, University of Puerto Rico at Humacao, CUH Station, Humacao, PR 00791, (2) Department of Chemistry, University of Puerto Rico - Rio Piedras, PR
The use of enzymes in organic solvent offers numerous advantages in the chemical synthesis of chiral compounds. However, a decrease in the catalytic activity is often observed in organic solvents. The use of different additives for enhancing enzyme activity has been a common practice in this area. In our lab, it was found that the lyophilization of the serine protease Subtilisin Carlsberg in the presence of methyl â cyclodextrin (MâCD) leads to a drastic enhancement in the activity and enantioselectivity of the enzyme. FTIR experiments showed that the additive helps to preserve the enzyme-native structure during lyophilization and subsequent exposure to organic solvents. Light-scattering experiments also showed that the additive reduces the aggregation of enzyme, leading to decreased mass-transfer limitations and a consequent increase in activity.
 

New Reactions and Methodology, Bioorganic Chemistry, Molecular Recognition and Self Assembly
8:00 PM-10:00 PM, Tuesday, 28 March 2006 Georgia World Congress Center -- Ex. Hall B4, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, 27 March 2006 Georgia World Congress Center -- Ex. Hall B4, Sci-Mix

Division of Organic Chemistry

The 231st ACS National Meeting, Atlanta, GA, March 26-30, 2006