Novel antifoulants: Inhibition of larval attachment by proteases

Sergey Dobretsov, Hairong Xiong, Ying Xu, Lisa A. Levin, Pei Yuan Qian

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70 Citations (Scopus)

Abstract

We investigated the effect of commercially available enzymes (α-amylase, α-galactosidase, papain, trypsin, and lipase) as well as proteases from deep-sea bacteria on the larval attachment of the bryozoan Bugula neritina L. The 50% effective concentrations (EC 50) of the commercial proteases were 10 times lower than those of other enzymes. Crude proteases from six deep-sea Pseudoalteromonas species significantly decreased larval attachment at concentrations of 0.03 to 1 mIU ml -1. The EC 50 of the pure protease from the bacterium Pseudoalteromonas issachenkonii UST041101-043 was close to 1 ng ml -1 (0.1 mIU ml -1). The protease and trypsin individually incorporated in a water-soluble paint matrix inhibited biofouling in a field experiment. There are certain correlations between production of proteases by bacterial films and inhibition of larval attachment. None of the bacteria with biofilms that induced attachment of B. neritina produced proteolytic enzymes, whereas most of the bacteria that formed inhibitive biofilms produced proteases. Our investigation demonstrated the potential use of proteolytic enzymes for antifouling defense.

Original languageEnglish
Pages (from-to)388-397
Number of pages10
JournalMarine Biotechnology
Volume9
Issue number3
DOIs
Publication statusPublished - May 2007

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Keywords

  • Antifouling
  • Deep-sea bacteria
  • Enzymes
  • Larval attachment
  • Proteases
  • Settlement

ASJC Scopus subject areas

  • Aquatic Science
  • Biotechnology
  • Biochemistry

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