Publikationsdatum:
2014-09-24
Beschreibung:
ICE BINDING PROTEINS FROM SEA ICE ALGAE
Sea ice is mainly a two-phase system, and its porous structure is largely determinant for biological activity within ice. During ice formation, solutes in the seawater are excluded from the ice matrix and segregate into brine droplets or brine channels, generally defined as brine inclusions inside sea ice. Outflow of high salinity brine and inflow of seawater of lower salinity, as well as further cooling, cause brine inclusions to narrow and eventually separate into individual pockets divided by ice bridges.
Despite the harsh conditions that govern within sea ice, where temperatures range from about -1.8°C on the bottom to -20°C or less on the top, and brine salinities can be as high as 200 on the Practical Salinity Scale, brine inclusions offer a habitat for a variety of microalgae. These algae play a crucial role for the ecology of the Polar Oceans, since they represent a concentrated food source in the low-productivity ice-covered sea, and in the months of melting they initiate blooms by seeding the water column. Algae have been found distributed within brine inclusions throughout the entire thickness of the ice column.
The strategies adopted by ice microorganisms to cope with conditions in sea ice remain to be unraveled. Recent studies showed that several organisms that populate sea ice, spreading from bacteria to diatoms and a crustacean species, have ice binding proteins (IBPs). These proteins are common in polar species, but lack in temperate organisms, suggesting that IBPs play a key role in adaptation to subzero conditions. The nomenclature of these proteins varies, depending on authors, from ice binding to antifreeze or ice structuring. In the generally accepted adsorption–inhibition model describing the mechanism of action of IBPs, proteins bind to the ice lattice and locally inhibit ice growth by the Gibbs-Thomson effect. Recent publications showed that some IBPs organize water molecules into an ice-like structure that matches defined planes of the ice crystal and is then gradually frozen to the ice lattice. One of the most prominent and best described effects of IBPs is thermal hysteresis, which describes the lowering of the freezing point of a solution below the melting point. Another effect which defines IBPs is inhibition of recrystallization, which is the grain boundary migration resulting in a growth of larger crystals at the expenses of small grains.
The biological role of IBPs from sea ice microalgae remains an open question. The importance of some IBP families, as observed in fishes or insects, lies in lowering the freezing point below environmental temperature, in order to avoid ice formation in cells or organs. Other IBPs have the function to inhibit recrystallization, as it has been suggested for plant IBPs. In the context of sea ice, it seems unlikely that the biological role of IBPs may be thermal hysteresis (measured in the order of 1°C) or recrystallization inhibition. Most of the IBPs from sea ice algae are active extracellularly. It has been suggested that they are trapped and accumulate within a layer of extracellular polysaccharide substances (EPS) secreted by several sea ice organisms. Microalgal IBPs produced recombinantly or collected from spent growth medium affect the structure of ice surface, causing pitting and characteristic microstructural features. This suggests that the proteins shape their frozen environment in order to increase their habitable space within sea ice.
However, the characterization of IBPs is of relevance not only to understand their functional role in sea ice, but also in the frame of possible applications of IBPs in the medical field, in the food industry and in other fields related to a control of ice crystals.
In the following we present some standard techniques to determine the protein activity in terms of thermal hysteresis (TH) and recrystallization inhibition (RI), which define the proteins as ice binding. Also, we present further methods (ice pitting assay, determination of the nucleating temperature) to characterize the activity of IBPs.
Repository-Name:
EPIC Alfred Wegener Institut
Materialart:
Inbook
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peerRev
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