Ice structuring proteins

Bindslev-Jensen, C., Sten, E., Earl, L., Crevel, R. W. R., Bindslev-Jensen, U., Hansen, T. K., Stahl Skov, R, and Poulsen, L. K. 2003. Assessment of the potential allergenicity of ice structuring protein type m HPLC 12 using the FAOAVHO 2001 decision tree for novel foods. Food Chem Toxicol 41(l) 81-87. 

IP3—inositol 1,4,5-triphosphate ISP—ice structuring protein IT—informatic technology... 

Xu H-N., Huang W., Jia C., Kim Y., Liu H. Evaluation of water holding capacity and breadmaking properties for frozen dough containing ice structuring proteins from winter wheat. Journal of Cereal Science 2009 49(2) 250-253. 

BaderschneiderB, CrevelRWR, EarlLK, LalljieA, Sanders DJ, Sanders D (2002). Sequence analysis and resistance to pepsin hydrolysis as part of an assessment of the potential allergenicity of ice structuring protein type III HPLC 12. Food Chem. Toxicol, 40 965-978. 

Savage, H. 1986. Water structure in crystalline solids Ices to proteins. In Water Science Reviews 2 Crystalline Hydrates (F. Franks, ed.), pp. 67-148. Cambridge Univ. Press, Cambridge, UK. 

Liou, Y. C., Tocilj, A., Davies, P. L., andjia, Z. (2000). Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature 406, 322-324. 

Antifreeze proteins (AFPs) are ice-binding proteins found in some organisms (such as fish, insects, plants and soil bacteria) that live at the temperature of their surroundings and encounter freezing conditions. AFPs help organisms to survive below 0°C by inhibiting ice growth. AFPs are structurally diverse, each is radically different from the others in its primary,... 

Savage HFJ (1986) Water structure in crystalline solids ices to proteins. Water Science Reviews 2 67-147... 

Morris, J., Morris, G. J., Taylor, R., Zhai, S., Slater, N. K. H., 2004. The effect of controlled nucleation on ice structure, drying rate and protein recovery in vials in a modified freeze dryer. Cryobiology 49 308-309. 

H. Chao, F.D. Sonnischen, C.L DeLuca, B.D. Sykes, and P.L. Davies, Structure-function relationship in the globular type III antifreeze protein Identification of a cluster of surface residues required for ice binding. Protein Science. 3 (1994) 1760. 

Thirdly, a stable icing foam requires a tendency for the surface of the extended protein film to solidify, thereby giving structure and permanence to the foam. Egg albumen is a hydrophilic (water-loving) colloid, for it is readily soluble in water. However, when subjected to heat, egg albumen becomes insoluble in water or is said to be hydrophobic (water-hating). Through this phenomenon of changing solubility, egg whites make very stable foams if used at sufficient concentration. 

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