A Bioengineered Glycosyl Hydrolase Effectively Disrupts Campylobacter jejuni Biofilms
TL;DR
Results indicate that CAase effectively disrupts multiple components of C. jejuni biofilm architecture despite lacking direct antimicrobial activity, suggesting potential utility in poultry-processing or surface-sanitation applications where targeted enzymatic disruption could enhance cleaning efficacy.
Abstract
Biofilms contribute significantly to the persistence and transmission of Campylobacter jejuni, yet enzymatic strategies for disrupting these structures remain underexplored. In this study, we evaluated the activity of a glycosyl hydrolase, CAase, against both planktonic and biofilm-associated C. jejuni. CAase showed no inhibitory effect on planktonic growth at concentrations up to 1 mg/mL. However, at 0.1 mg/mL, CAase reduced mature biofilm biomass by more than 93% in the wild-type strain and produced similar reductions in a luxS mutant, demonstrating substantial degradation of conserved glycan components within the extracellular polymeric substance (EPS). Scanning electron microscopy (SEM) imaging revealed substantial extracellular matrix loss, structural disruption, and altered cell morphology following CAase treatment. Rheological measurements demonstrated marked decreases in kinematic viscosity, further reflecting weakened biofilm cohesion. Together, these results indicate that CAase effectively disrupts multiple components of C. jejuni biofilm architecture despite lacking direct antimicrobial activity. This level of biofilm removal suggests potential utility in poultry-processing or surface-sanitation applications where targeted enzymatic disruption could enhance cleaning efficacy.