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Influence of subtilisin on the adhesion of a marine bacterium which produces mainly proteins as extracellular polymers
Author(s) -
Leroy C.,
Delbarre C.,
Ghillebaert F.,
Compere C.,
Combes D.
Publication year - 2008
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1111/j.1365-2672.2008.03837.x
Subject(s) - library science , subtilisin , art , microbiology and biotechnology , chemistry , art history , biology , computer science , biochemistry , enzyme
Aims: The nature of exopolymers involved in the adhesion of a marine biofilm‐forming bacterium Pseudoalteromonas sp. D41 was investigated to evaluate and understand the antifouling potential of subtilisin. Methods and Results: The exopolymers of D41 produced by fermentation were analysed by FTIR and SDS‐PAGE showing the presence of polysaccharides, glycoproteins and proteins. A high content of proteins was detected both in soluble and capsular fractions. The microscopic observations of fluorescamine and calcofluor stained adhered D41 indicated mainly the presence of proteins in exopolymers produced during adhesion. Subtilisin, the broad spectrum protease, tested in natural sea water and in polystyrene microplates showed that antifouling activity was higher in the prevention of bacterial adhesion than in the detachment of adhered D41 cells. Conclusions: Overall, these results demonstrate the involvement of proteins in Pseudoalteromonas sp . D41 adhesion and confirm the high antifouling potential of subtilisin. Significance and Impact of the Study: This study emphasizes the major role of proteins instead of polysaccharides, thus extending our knowledge regarding the nature of extracellular polymers involved in bacterial adhesion. Furthermore, the high antifouling potential of subtilisin evaluated in the very first stages of fouling, bacterial adhesion, could lead to less toxic compounds than organometallic compounds in antifouling paint.