The ChiA protein from Serratia marcescens is responsible for hydrolysis of 1,4 glycosidic bonds in N-acetyl-glucosamine chains, that comprise chitin. Chitin, being the second most abundant polymer, has untouched potential as a source for biofuel feedstocks. Here we aim to enhance chitinase activity through displaying the ChiA protein on the surface layer proteins (S-layers) of Caulobacter vibrioides. The S-layer of C. vibrioides is a nanometer scale hexagonal 2-D crystalline lattice composed of a single protein, RsaA, and covers the entire surface of the organism. In this study, the chiA gene isolated from S. marcescens was designed and amplified for expression in the C. vibrioides S-layer.
Louis Stokes Alliance for Minority Participation (LSAMP) Scholarship