不凍タンパク質の予熱と凝集による氷成長抑制の向上

抄録

We conducted measurements on unidirectional freezing for antifreeze-protein solution either preheated or pH-controlled in a narrow space. The interface temperature was measured with a thermocouple. The turbidity of the preheated solution was measured with a ultra-violet and visible spectrophotometer. It was found from the results for the turbidity measurement that the preheated antifreeze protein formed aggregates. The interface temperature for the preheated solution was lower than that for the unheated solution. In addition, the interface temperature for the solution with its pH controlled to isoelectric point was lower than that for the solution without control.