The serine protease Esperase HPF inhibits the formation of multispecies biofilm

Hangler, Martin; Burmølle, Mette; Schneider, Ib; Allermann, K.; Jensen, Bo

doi:10.1080/08927010903096008

Cited by 26 publications

(15 citation statements)

References 36 publications

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“…D41 (Leroy et al 2008b). In contrast, the enzyme inhibitory effects were comparable to the detachment effects for a multispecies biofilm (Hangler et al 2009) suggesting that, in this case, the enzyme effectively degrades both protein-based adhesives and proteins contained in the matrix (Hangler et al 2009). Recent work also showed that differences in chemical composition of the EPS are reflected on the vulnerability of biofilms to enzymatic treatment (Lequette et al 2010;Chaignon et al 2007;Augustin et al 2004).…”

Section: Insert Figurementioning

confidence: 92%

Immobilized enzymes affect biofilm formation

2011

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The effect of the activity of immobilized enzymes on the initial attachment of pathogenic bacteria commonly associated with nosocomial infections (Pseudomonas aeruginosa and Staphylococcus epidermidis) was investigated. The proteolytic enzymes, subtilisin A and the glycoside hydrolase cellulose, were covalently attached onto poly(ethylene-alt-maleic) anhydride copolymer films. A comparison between active and heatinactivated surfaces showed that while the activity of immobilized cellulase reduced the attachment of S. epidermidis by 67%, it had no effect on the attachment of P. aeruginosa. Immobilized subtilisin A had opposite effects: the active enzyme had no effect on the attachment of S. epidermidis but reduced the attachment of P. aeruginosa by 44%. The results suggest that different biomolecules are involved in the initial steps of attachment of different bacteria, and that the development of broad-spectrum antifouling enzymatic coatings will need to involve the co-immobilization of enzymes.

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Section: Insert Figurementioning

confidence: 92%

Immobilized enzymes affect biofilm formation

2011

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“…D41, suggesting its ineffectiveness on structural composition of the biofilm matrix. In contrast, Hangler et al [15] observed that the serine protease Esperase HPF (subtilisin) affected both the attachment and the detachment of a multispecies biofilm, suggesting that, in this case, the enzyme effectively degraded both protein-based adhesives and proteins contained in the matrix. Recent work also showed that differences in the chemical composition of the EPS are reflected in the vulnerability of biofilms to enzymatic treatments [2,7,25].…”

Section: Resultsmentioning

confidence: 87%

Immobilized Hydrolytic Enzymes Exhibit Antibiofilm Activity Against Escherichia coli at Sub-Lethal Concentrations

et al. 2015

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The effects of two commercially available immobilized enzymes (namely the glycosidase pectinase and the protease subtilisin A) at sub-lethal concentrations were investigated in terms of their influence on biofilm genesis, on the composition of the biofilm matrix, and their antibiotic synergy against Escherichia coli biofilm, used as a model system of bacterial biofilms. The best antibiofilm performance of solid-supported hydrolases was obtained at the surface concentration of 0.022 and 0.095 U/cm(2) with a reduction of 1.2 and 2.3 log CFU/biofilm for pectinase and subtilisin, respectively. At these enzyme surface concentrations, the biocatalysts affected the structural composition of the biofilm matrix, impacting biofilm thickness. Finally, the immobilized hydrolases enhanced biofilm sensitivity to a clinically relevant concentration of the antibiotic ampicillin. At the final antibiotic concentration of 0.1 mg/ml, a reduction of 2 and 3.5 log10 units in presence of 0.022 Upectinase/cm(2) and 0.095 Usubtilisin/cm(2) was obtained, respectively, in comparison the antibiotic alone. Immobilized pectinase and subtilisin at sub-lethal concentrations demonstrated a great potential for antibiofilm applications.

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“…One Gram positive bacterium namely Microbacterium phyllosphaerae and three Gram negative bacterial strains namely, Shewanella japonica, Dokdonia donghaensis and Acinetobacter lwoffii were all isolated from green alga Ulva australis. The effects of time and amount of Esperase HPF, was tested on the robustness and the oxidative metabolism of biofilm developed in 96 well plates [30]. Esperase HPF did not inhibit the oxidative metabolism of the bacterial biofilm or inhibit planktonic growth, but the enzyme inhibited biofilm formation by its proteolytic activity and heat inactivated enzyme had no effect.…”

Section: Use Of Commercially Available Proteases As Antibiofilm Agentsmentioning

confidence: 99%

“…The antifouling (AF) potential of the serine protease Esperase HPF (subtilisin) was evaluated by Hangler et al [30] for its ability to prevent the biofilm formation of a four-species bacterial species. One Gram positive bacterium namely Microbacterium phyllosphaerae and three Gram negative bacterial strains namely, Shewanella japonica, Dokdonia donghaensis and Acinetobacter lwoffii were all isolated from green alga Ulva australis.…”

Section: Use Of Commercially Available Proteases As Antibiofilm Agentsmentioning

confidence: 99%

“…Esperase HPF did not inhibit the oxidative metabolism of the bacterial biofilm or inhibit planktonic growth, but the enzyme inhibited biofilm formation by its proteolytic activity and heat inactivated enzyme had no effect. The enzyme concentration causing maximum biofilm inhibition in case of the different test organisms was determined after 72 hours [30].…”

Section: Use Of Commercially Available Proteases As Antibiofilm Agentsmentioning

confidence: 99%

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Role of Extracellular Proteases in Biofilm Disruption of Gram Positive Bacteria with Special Emphasis on Staphylococcus aureus Biofilms

A¹

2014

Enz Eng

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Bacterial biofilms are multicellular structures akin to citadels which have individual bacterial cells embedded within a matrix of a self-synthesized polymeric or proteinaceous material. Since biofilms can establish themselves on both biotic and abiotic surfaces and that bacteria residing in these complex molecular structures are much more resistant to antimicrobial agents than their planktonic equivalents, makes these entities a medical and economic nuisance. Of late, several strategies have been investigated that intend to provide a sustainable solution to treat this problem. More recently role of extracellular proteases in disruption of already established bacterial biofilms and in prevention of biofilm formation itself has been demonstrated. The present review aims to collectively highlight the role of bacterial extracellular proteases in biofilm disruption of Gram positive bacteria. The article includes description of anti-biofilm activity of both endogenously produced extracellular proteases as well as extraneously applied proteases against biofilms formed by important Gram positive pathogens.

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The serine protease Esperase HPF inhibits the formation of multispecies biofilm

Cited by 26 publications

References 36 publications

Immobilized enzymes affect biofilm formation

Immobilized enzymes affect biofilm formation

Immobilized Hydrolytic Enzymes Exhibit Antibiofilm Activity Against Escherichia coli at Sub-Lethal Concentrations

Role of Extracellular Proteases in Biofilm Disruption of Gram Positive Bacteria with Special Emphasis on Staphylococcus aureus Biofilms

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