Bacterial biofilms consist of surface attached bacteria encased in an extracellular polymeric substance (EPS) composed of exported polysaccharides, proteins and extracellular DNA that facilitates both cell–cell and cell–surface attachment and serves as a protective barrier for the encased cells. Infections by these biofilm forming bacteria are a major health challenge costing an estimated additional $11 billion in health care costs in the USA annually. The biofilm EPS serves as a protective barrier increasing resistance to common antibiotics used to treat bacterial infections. Thus, enzymes that breakdown of biofilm EPS components combined with antibiotic therapy has emerged as a promising strategy to disrupt and treat biofilms. The EPS of many bacterial species are rich in exopolysaccharides and one of the most common is de-N-acetylated β-(1→6)-poly-N-acetylglucosamine (dPNAG), found in the EPS of both gram-positive and gram-negative human pathogens, including Staphylococcus epidermidis and Staphylococcus aureus. There are only two enzymes that are known to specifically recognize and catalyze the hydrolysis of dPNAG, and both have relatively slow catalytic activity. Enzymes with improved dPNAG hydrolase activity have potential use as biofilm dispersal agents. Here, we report colorimetric and fluorogenic dPNAG probes that enable the high-throughput identification and characterization of dPNAG hydrolyzing enzymes and a platform for the high-throughput engineering of biofilm hydrolase enzymes.

Platform for engineering bacterial biofilm glycosyl hydrolase enzymes

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.