title: Salt-induced enhancement of antifreeze protein activity: a salting-out effect.
abstract: Antifreeze proteins are a structurally diverse group of proteins characterized by their unique ability to cause a separation of the melting- and growth-temperatures of ice. These proteins have evolved independently in different kinds of cold-adapted ectothermic animals, including insects and fish, where they protect against lethal freezing of the body fluids. There is a great variability in the capacity of different kinds of antifreeze proteins to evoke the antifreeze effect, but the basis of these differences is not well understood. This study reports on salt-induced enhancement of the antifreeze activity of an antifreeze protein from the longhorn beetle Rhagium inquisitor (L.). The results imply that antifreeze activity is predetermined by a steady-state distribution of the antifreeze protein between the solution and the ice surface region. The observed salt-induced enhancement of the antifreeze activity compares qualitatively and quantitatively with salt-induced lowering of protein solubility. Thus, salts apparently enhance antifreeze activity by evoking a solubility-induced shift in the distribution pattern of the antifreeze proteins in favour of the ice. These results indicate that the solubility of antifreeze proteins in the solution surrounding the ice crystal is a fundamental physiochemical property in relation to their antifreeze potency.
authors.affiliation: Department of Biology, Norwegian University of Science and Technology (NTNU), Høgskoleringen 5, 7491 Trondheim, Norway. Erlend.Kristiansen@bio.ntnu.no
authors.forename: Erlend
authors.initials: E
authors.lastname: Kristiansen
authors.forename: Sindre Andre
authors.initials: SA
authors.lastname: Pedersen
authors.forename: Karl Erik
authors.initials: KE
authors.lastname: Zachariassen
mesh_terms: D000818:Animals; D021301:Antifreeze Proteins / Q000737:chemistry / Q000502:physiology*; D001517:Coleoptera / Q000737:chemistry*; D003460:Crystallization; D006458:Hemolymph / Q000737:chemistry / Q000378:metabolism; D007053:Ice; D008954:Models, Biological; D011485:Protein Binding; D012492:Salts / Q000737:chemistry*; D012995:Solubility
chemical_list: D021301:Antifreeze Proteins; D007053:Ice; D012492:Salts