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Slideshow

Establish enzyme complex with polymer and DNA scaffolds to improve enzyme catalytic activity and thermal stability

Xue Wang
Xue Wang
Department of Chemistry
University of Georgia
ONLINE ONLY
Analytical Seminar

Enzymes are natural catalysts that orchestrate metabolic processes in live cells. Because of their high efficiency, selectivity, and biocompatibility, the applications of these catalysts were extended to many industrial and biomedical technologies for chemical synthesis, biofuel production and food industries. Here I will present my research on modification of lysozyme and cellulases with polymer and DNA scaffolds, where the enzyme complex would be more suitable with industrial applications. Elevated temperatures are always used for many applications to increase rates of the processes and decrease bacterial contaminations. However, most mesophilic enzymes denature at temperatures above 50−60 °C due to unfolding of the protein molecules. A “grafting through” conjugation strategy was designed to improve lysozyme catalytic activity and thermal stability by the synthesis of a synthetic polymer−enzyme hybrid. Polyethylene glycol (PEG) polymers have also been mixed with lysozyme to understand the structural and conformational effects on enzyme stability at high temperature. Cellulosomes are bacterial protein complexes that bind and efficiently degrade lignocellulosic substrates. To be better compatible with industrial applications, a creation of artificial cellulosome based on DNA scaffold was developed to illustrate the synergy effect of enzymatic complexes and discover impacts of sequence and spatial arrangement of enzymes in the complex.

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