Biofouling is the accumulation of sessile marine organisms, such as algae, tube worms and barnacles on man-made substrata and has negative economic and ecological implications. Ship hulls are readily fouled, which significantly increases drag while decreasing ship fuel efficiency when moving through water. Fouled hulls have also become important vectors of invasive species. These problems are minimized when hulls are painted with a toxic anti-fouling or non-toxic foul-release coating. Due to recent restrictions of anti-fouling paint use, research and development of non-toxic alternatives has increased.
Novel hull coating efficiency is often quantified by the critical removal stress value of barnacles from the coating. Barnacle adhesive cement protein content is thought to be responsible for barnacles’ incredible ability to adhere underwater. The expression level and type of adhesive proteins has eluded scientists due to their extreme insolubility within cured barnacle cement. Identification of these proteins may provide insight to the adhesion of fouling species and aid coating development.
Barnacles are a cosmopolitan organism, able to withstand a wide range of environmental conditions, yet foul-release coating research had not previously incorporated environmental factors as variables in determining coating performance. Temperature is known to affect protein structure and function and is also a formative factor of barnacle larvae survival and development. Even so, the interaction between temperature and barnacle adhesion to has not previously been explored. We examined the effect of temperature on barnacle adhesion to foul-release coatings. After observing differences in critical removal stress due to temperature, we attempted to attribute these differences to specific proteins within the adhesive using 2D SDS PAGE. Gel image analysis determined that there were significant differences in cement protein expression between barnacles raised within different temperatures. Preliminary protein identification with Mass Spectronomy (MALDI TOF/TOF) was performed, however further research and a larger barnacle genomic database is needed to elucidate barnacle cement protein sequences.
| Identifer | oai:union.ndltd.org:CALPOLY/oai:digitalcommons.calpoly.edu:theses-1254 |
| Date | 01 March 2010 |
| Creators | Johnston, Laurel A |
| Publisher | DigitalCommons@CalPoly |
| Source Sets | California Polytechnic State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Master's Theses |
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