Enzymatic Approaches to Biofilm Control

The persistence of microbial biofilms is largely due to the resilience of the extracellular polymeric substance (EPS) matrix that encases cells on biotic and abiotic surfaces. Enzymatic approaches target key matrix components—polysaccharides, nucleic acids and proteins—with a precision that complements or supersedes traditional antimicrobials. Glycoside hydrolases such as glucanases, dextranases and mutanases cleave polysaccharide linkages in fungal and bacterial biofilms, while DNases degrade extracellular DNA scaffolds. Proteases and polysaccharide lyases further disrupt mechanical integrity, enhancing antimicrobial penetration and immune clearance. Quorum-quenching enzymes inhibit signalling pathways to prevent biofilm maturation. Advances in enzyme discovery, structural characterisation and protein engineering have yielded catalysts with enhanced stability, substrate specificity and biocompatibility. Formulation strategies—such as encapsulation, immobilisation and fusion to targeting domains—improve delivery to biofilm niches. Such enzymatic interventions show promise across healthcare, food processing and marine fouling, offering sustainable, resistance-mitigating solutions to a global biofilm challenge.

Research from Nature Portfolio

Recent studies have illuminated the structural and functional attributes of GH87 α-1,3-glucanases that degrade biofilm polysaccharides. A newly characterised enzyme from Flavobacterium sp. EK-14 exhibits exceptional hydrolytic activity against α-1,3-glucan under physiologically relevant conditions, releasing oligosaccharides and glucose with minimal off-target effects. This enzyme features a multipartite architecture including lectin-like domains that enhance substrate recognition and a secretion motif that facilitates extracellular deployment. In parallel, high-resolution crystallography of the catalytic unit of a GH87 α-1,3-glucanase from Bacillus circulans has revealed tandem domain organisation—a galactose-binding-like motif coupled to a β-helix–type catalytic core. Key aspartate residues lining the substrate-binding cleft have been identified, offering targets for rational mutagenesis to optimise activity against biofilm-associated glucans. These insights pave the way for engineering glucanases as specific biofilm disrupters in medical and industrial applications.

Enzymatic Approaches to Biofilm Control publication trend

The graph below shows the total number of articles in enzymatic approaches to biofilm control across all publications each year (not limited to Nature Index journals).

Technical terms

Extracellular polymeric substance (EPS): The complex mixture of polysaccharides, proteins, nucleic acids and lipids forming the biofilm matrix.

Glycoside hydrolase: An enzyme that catalyses the hydrolysis of glycosidic bonds in carbohydrates.

α-1,3-Glucanase: A glycoside hydrolase targeting α-1,3-linked glucose residues in glucan polymers.

Dextranase: An enzyme that degrades α-1,6-linked glucose polymers (dextrans) present in biofilms.

Mutanase: A specialised glucanase that hydrolyses Streptococcus mutans–derived α-1,3-glucan (mutan).

Carbohydrate-binding module (CBM): A protein domain that enhances enzyme affinity for specific polysaccharide substrates.

References

1. α-1,3-Glucanase from the gram-negative bacterium Flavobacterium sp. EK-14 hydrolyzes fungal cell wall α-1,3-glucan. Scientific Reports (2023).
2. Crystal structure of the catalytic unit of GH 87-type α-1,3-glucanase Agl-KA from Bacillus circulans. Scientific Reports (2019).
3. Biochemical Analysis of Recombinant Fungal Mutanases A NEW FAMILY OF α1,3-GLUCANASES WITH NOVEL CARBOHYDRATE-BINDING DOMAINS*. Journal of Biological Chemistry (2000).
4. Enzymes That Hydrolyze Fungal Cell Wall Polysaccharides I. PURIFICATION AND PROPERTIES OF AN ENDO-α-d-(1 → 3)-GLUCANASE FROM TRICHODERMA VIRIDE. Journal of Biological Chemistry (1969).
5. Marine Bacterial Dextranases: Fundamentals and Applications. Molecules (2022).