Abstract
Biochemical and molecular biological studies on Limnoperna fortunei adhesive proteins indicate that marine and freshwater mussels share several essential molecular traits involving oxidation of tyrosine residues to generate both adhesive force (surface coupling) and cohesive force (protein cross-linking in adhesive plaque matrices). The amino acid compositions of freshwater mussels show higher levels of electrolytic residues, such as aspartic and glutamic acids. With the purpose of developing antifouling strategies based on the knowledge of the adhesive mechanism of L. fortunei, several laboratory experiments have been conducted that minimize polar or hydrogen-bonding surface components. Chemical modifications and substrate coatings were investigated to search for low-energy surfaces and examine biocidal effects of metal ions. Field experiments indicate that water flow velocity is correlated with the attachment force of young, newly recruited mussels, and provide useful information on sites most vulnerable to mussel fouling in water treatment facilities.
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Acknowledgements
The authors thank Dr. Isamu Sakaguchi and Takuya Kobayashi, CRIEPI, for supplying the L. fortunei foot samples, which were used in the molecular cloning experiments. This work was supported by Grants-in-Aid No. 26288101, and partly by the Japanese Association for Marine Biology (JAMBIO) No 23–73.
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Ohkawa, K., Nomura, T. (2015). Control of Limnoperna fortunei Fouling: Antifouling Materials and Coatings. In: Boltovskoy, D. (eds) Limnoperna Fortunei. Invading Nature - Springer Series in Invasion Ecology, vol 10. Springer, Cham. https://doi.org/10.1007/978-3-319-13494-9_22
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DOI: https://doi.org/10.1007/978-3-319-13494-9_22
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