Differential Scanning Calorimetric and Circular Dichroistic Studies on Plant Antifreeze Proteins

Antifreeze protein (AFP) can lower the freezing point by inhibiting the growth of ice crystals. In this article, the thermal hysteresis activity (THA) of a plant AFP was measured with differential scanning calorimetry (DSC). As is shown, when the amount of ice in the sample was less than 5% THA of this AFP reached as high as 0.35°C. The secondary structure of this AFP was studied with circular dichroism (CD). The CD spectrum from 195to 240 nm indicated a well-defined secondary structure consisting 11% α-helix, 34%antiparallel β-sheet and 55% random coil.