Isolation, purification, and characterization of an antifreeze protein from the sea smelt (Hypomesus japonicus)

CHED 217

Ayanah Duhaney, ayduhaney@mail.widener.edu, Mohit Sirohi, msirohi@mail.widener.edu, and Loyd D. Bastin, bastin@pop1.science.widener.edu. Department of Chemistry, Widener University, One University Place, Chester, PA 19013-5792
Many organisms are able to survive at nearly subzero temperatures. However, at these temperatures, bodily fluids are normally susceptible to freezing. Consequently, numerous organisms have adapted to these lower temperatures through the synthesis of antifreeze proteins. Antifreeze proteins are proteins capable of binding to ice thus making further ice crystal growth energetically unfavorable; therefore, depressing the freezing point non-colligatively and allowing the organism to endure harsher conditions. The sea smelt is capable of surviving frigid temperatures. Here, we report the isolation, purification, and thermodynamic studies of an antifreeze protein from the muscle of sea smelt. Through the study of the structure and function of antifreeze proteins, we hope to determine the mechanism by which proteins inhibit ice crystal growth in the sea smelt.