Extraction, purification, and characterization of green mussel perna viridis foot protein-3 (PVFP-3)

• Main Author: Chin, Peter Tse Nam
• Other Authors: School of Materials Science and Engineering
• Format: Final Year Project
• Language: English
• Published: 2011
• Subjects: DRNTU::Engineering::Materials
• Online Access: http://hdl.handle.net/10356/44479
• Institution: Nanyang Technological University

Biofouling is a big problem in many parts of the world often causing large economic loss in rectifying the damage done. Preventing biofouling through the use of coatings in industries as varied as shipping and power generation to mariculture is of major interest. While it is recognised that a universal coating to protect against all fouling species is unlikely, detailed studies of the adhesion mechanisms of fouling organisms is crucial to tailor anti-fouling mechanisms to specific species that cause the greatest amount of economic loss, while minimizing environmental impact by restricting the use of generally toxic but highly effective multispecies antifouling coatings that exist today. The adhesion of the green mussel Perna viridis is thus studied to better understand its adhesion properties by understanding the protein composition of its adhesive plaque. This project targets specifically foot protein 3 which is believed, through studies on other species, to be a main contributor to the success of mussel adhesion. Initial efforts to isolate the protein were met with negative results, but minor modifications to the purification protocol have shown improved crude extract yields of a 5.3kDa protein that is similar in weight to previously identified proteins in the adhesive plaque. The suspect protein is appears to match the migration pattern on acid-urea gel assays of a suspected adhesive plaque protein identified by Ohkawa [35] for Perna viridis. Current high performance liquid chromatography experiments in our lab have also indicated a greater degree of hydrophobicity for PVFP-3 proteins compared to its Mytilus Edulis counterpart.