Structure and function of subtilisin NPB' solubilized in organic solvents

摘要

Enzyme structure and function have been studied for subtilisin NPB' solubilized in organic solvents solvents by ion pairing with low concentrations of an anionic surfactant (Aerosol OT) in the absence of reversed micelles. Soluble subtilisin shows strikingly different behavior in octane and tetrahydrofuran (THF). In octane, the K_cat/K_m for the transesterification of N-acetyl-L-phenylalanine ethyl ester (APEE) is 370 M~-1S~-1, within one order of magnitude of the enzyme's hydrolytic activity in water.