抗冻蛋白
差示扫描量热法
粉虱
冰晶
冰点
防冻剂
化学
结晶学
氨基酸
食品科学
生物物理学
生物
热力学
生物化学
生态学
幼虫
物理
有机化学
光学
作者
Torben Hansen,John G. Baust
标识
DOI:10.1016/0167-4838(88)90275-0
摘要
Antifreeze proteins (AFP) are able to inhibit the growth of ice-crystals at temperatures below the equilibrium freezing point (Tf) of hemolymph. The analysis of AFP activity has commonly involved the use of direct microscopic observation of a sample following inoculation with ice. The resulting activity, defined as the amount of thermal hysteresis observed between Tf and the subsequent rapid growth of ice, has been reported to range up to 7° C. However, most studies report high level of variation, possibly due to ice-crystal size variability and the presence of non-visible ice nuclei. We describe a new method of analysis of AFP activity using differential scanning calorimetry (DSC). DSC analysis reveals much higher activity, up to 10° C, with less variation observed within a sample, and is not subject to the difficulty of accurate assessment of ice-crystal volume.
科研通智能强力驱动
Strongly Powered by AbleSci AI