HYDROPHOBILIZATION OF AN ESTERASE BY GENETIC COMBINATION WITH POLYPROLINE AT THE CARBOXYL-TERMINAL

Polyproline, which is an amphiphilic polypeptide, was incorporated int o the carboxyl terminal of an esterase by the recombinant DNA techniqu e. The hydrophobicity of the esterase increased with increasing chain length of polyproline without inducing significant conformational chan ges. The mutant esterase catalyzed the hydrolysis of long-chain carbox ylic acid ester more efficiently than the native esterase. It is consi dered that the alteration of substrate specificity is due to enhanced access of the mutant esterases to hydrophobic substrates. (C) 1998 Joh n Wiley & Sons, Inc. Biotechnol Bioeng 59: 582-586, 1998.