Structural studies on novel thermophilic biocatalysts

Abstract

The thermostable enzymes pyroglutamyl carboxyl peptidase, L-aminoacylase and alcohol dehydrogenase have been cloned and over-expressed in Escherichia coli. The enzymes have potential for their use in industrial biocatalysis. Stuctural studies have aided our understanding of the mechanisms used for thermostability by these proteins. Site-specific mutations of the pyroglutamyl carboxyl peptidase where a cysteine involved in inter-subunit disulfide bond formation and a phenylalanine, leucine rich hydrophobic core have been removed or substituted, have provided some insight for the future engineering of more robust novel proteins for industrial bio-transformations.