Ice-Binding Proteins from Marine Bacteria, Yeast, and Microalgae: Types, Functions, and Application

Abstract

Ice-binding proteins (IBPs) are, literally, referred to a group of proteins that bind to ice crystals. IBPs encompass antifreeze proteins (AFPs), ice nucleation proteins (INPs), ice recrystallization protein, and ice anchoring protein and so on. In most cases IBPs and AFPs are interchangeable terms. IBPs, although structurally diverse, bind to the surface of ice crystals and control the growth of ice crystal growth. This binding causes difference of melting and freezing points, termed thermal hysteresis (TH) and ice recrystallization inhibition (RI). Extensive studies have shown that IBPs from fish, insects, and plants are very effective in ice RI. This ability seems to protect membranes from freezing injury and thus to help the organisms survive at extremely cold environments. Theses two intriguing activities, TH and RI, of IBPs have drawn interest from academia and industries because these proteins have broad potential applications, including cryopreservation, food preservation, transgenic technology, and cryosurgery. However the application is mainly hampered by lack of mass production of IBPs and/or AFPs.nd so on. In most cases IBPs and AFPs are interchangeable terms. IBPs, although structurally diverse, bind to the surface of ice crystals and control the growth of ice crystal growth. This binding causes difference of melting and freezing points, termed thermal hysteresis (TH) and ice recrystallization inhibition (RI). Extensive studies have shown that IBPs from fish, insects, and plants are very effective in ice RI. This ability seems to protect membranes from freezing injury and thus to help the organisms survive at extremely cold environments. Theses two intriguing activities, TH and RI, of IBPs have drawn interest from academia and industries because these proteins have broad potential applications, including cryopreservation, food preservation, transgenic technology, and cryosurgery. However the application is mainl