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The effects of a serine protease, Alcalase (R), on the adhesives of barnacle cyprids (Balanus amphitrite)

Lookup NU author(s): Dr Nicholas Aldred, Sheelagh Conlan, Professor Tony Clare

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Abstract

Barnacles are a persistent fouling problem in the marine environment, although their effects ( eg reduced fuel efficiency, increased corrosion) can be reduced through the application of antifouling or fouling-release coatings to marine structures. However, the developments of fouling-resistant coatings that are cost-effective and that are not deleterious to the marine environment are continually being sought. The incorporation of proteolytic enzymes into coatings has been suggested as one potential option. In this study, the efficacy of a commercially available serine endopeptidase, Alcalase (R) as an antifoulant is assessed and its mode of action on barnacle cypris larvae investigated. In situ atomic force microscopy (AFM) of barnacle cyprid adhesives during exposure to Alcalase supported the hypothesis that Alcalase reduces the effectiveness of the cyprid adhesives, rather than deterring the organisms from settling. Quantitative behavioural tracking of cyprids, using Ethovision (TM) 3.1, further supported this observation. Alcalase removed cyprid 'footprint' deposits from glass surfaces within 26 min, but cyprid permanent cement became resistant to attack by Alcalase within 15 h of expression, acquiring a crystalline appearance in its cured state. It is concluded that Alcalase has antifouling potential on the basis of its effects on cyprid footprints, un-cured permanent cement and its non-toxic mode of action, providing that it can be successfully incorporated into a coating.


Publication metadata

Author(s): Aldred N, Phang IY, Conlan SL, Clare AS, Vancso GJ

Publication type: Article

Publication status: Published

Journal: Biofouling

Year: 2008

Volume: 24

Issue: 2

Pages: 97-107

ISSN (print): 0892-7014

ISSN (electronic): 1026-7867

Publisher: Taylor & Francis Ltd.

URL: http://dx.doi.org/10.1080/08927010801885908

DOI: 10.1080/08927010801885908


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