Effects of commercial enzymes on the adhesion of a marine biofilm-forming bacterium

Type Article
Date 2008
Language English
Author(s) Leroy C.2, Delbarre Ladrat ChristineORCID2, Ghillebaert F.3, Compere ChantalORCID1, Combes D.4
Affiliation(s) 1 : IFREMER, Serv Interfaces & Capteurs, Brest, France.
2 : IFREMER, Lab Biotechnol & Mol Marines, Nantes, France.
3 : Mexel SA, Verberie, France.
4 : INSA, CNRS, INRA, Lab Biotechnol Bioprocedes,UMR 5504,UMR 792, Toulouse, France.
Source Biofouling (0892-7014) (Taylor & Francis), 2008 , Vol. 24 , N. 1 , P. 11-22
DOI 10.1080/08927010701784912
WOS© Times Cited 102
Keyword(s) Marine biofilm, Antifouling, Pseudoalteromonas, Enzymes, Adhesion
Abstract The antifouling potential of commercial hydrolases, four proteases, seven glycosidases and one lipase was evaluated on the adhesion of marine Pseudoalteromonas sp. D41. The experimental method, adapted to screen antifouling agents, was based on bacterial adhesion in natural sterile sea water in a microtiter plate and on total biomass quantification by the fluorescent dye DAPI (4[prime]6-diamidino-2-phenylindole). Savinase (subtilisin) was the most effective hydrolase in both the prevention of bacterial adhesion and the removal of adhered bacteria. However, some enzymatic preparations tested such as Amano protease were not only ineffective but also increased the number of adhered bacterial cells. Enumeration using epifluorescence microscopy of CTC (5-cyano-2,3-ditolyl tetrazolium chloride) and DAPI stained adhered D41 cells confirmed these observations. Overall, these results demonstrated that hydrolases could either prevent adhesion and remove adhered bacterial cells effectively, or conversely increase bacterial adhesion, depending on enzymatic concentrations and the type of enzymes tested.
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