Meyer J D, Kendrick B S, Matsuura J E, Ruth J A, Bryan P N, Manning M C
Department of Pharmaceutical Sciences, School of Pharmacy, University of Colorado Health Sciences Center, Denver, USA.
Int J Pept Protein Res. 1996 Mar;47(3):177-81. doi: 10.1111/j.1399-3011.1996.tb01342.x.
With very low concentrations of anionic detergents, such as sodium dodecyl sulfate (SDS) and Aerosol OT (AOT), it is possible to solubilize proteases in organic solvents, while retaining enzymatic activity. For example, the SDS-subtilisin BPN' complex catalyzes transesterification of Ac-Phe-OMe in ethanol with a kcat/Km of 36 M-1 s-1 for mutant M1 and 39 M-1 s-1 for the wild type. By comparison, M1 suspended in ethanol is approximately 1000-fold less active, with a kcat/Km of 0.03 M-1 s-1. Similarly, AOT complexes of alpha-chymotrypsin were found to be approximately 1000 times more active (kcat/Km = 100-350 M-1 s-1) than the suspended enzyme.
