Enhancement of ice growth inhibition by preheating and aggregation of antifreeze protein

Abstract

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.