Complex Formation Between Chymotrypsin and Ethyl Cellulose as a Means to Solubilize the Enzyme in Active Form in Toluene

Abstract

Chymotryspin and ethyl cellulose were mixed in an aqueous phosphate buffer solution and freeze dried. Due to complex formation between the substances it was possible to dissolve or at least finely disperse these preparations in toluene. The chymotrypsin-ethyl cellulose complexes were characterized by light scattering measurements. Complexes were also formed by mixing enzyme powder in toluene containing ethyl cellulose and buffer but this was a slow process. Experiments with radioactively labelled bovine serum albumin showed that this protein was also solubilized in toluene in the presence of ethyl cellulose and buffer salts. Chymotrypsin complexes were used to catalyze the esterification of N-acetyl-L-phenylalanine with ethanol in toluene. The presence of buffer salts greatly increased the initial reaction rate of the esterification reaction. The complexes were consideraly more active and stable than enzyme powder in toluene.