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首页> 外文期刊>Thermochimica Acta: An International Journal Concerned with the Broader Aspects of Thermochemistry and Its Applications to Chemical Problems >THE SUITABILITY OF SCANNING CALORIMETRY TO INVESTIGATE SLOW IRREVERSIBLE PROTEIN DENATURATION
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THE SUITABILITY OF SCANNING CALORIMETRY TO INVESTIGATE SLOW IRREVERSIBLE PROTEIN DENATURATION

机译：扫描量热法研究缓慢不可逆的蛋白质脱氢的适宜性

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The denaturation and aggregation of bovine beta-lactoglobulin (50 g/l) at neutral pH was investigated by scanning calorimetry. To cover a wide range of scan rates (2-1200 degrees C/h), we used three different calorimeters: two scanning calorimeters (PE DSC7 and Hart Scientific DSC 4207) and an adiabatic calorimeter. The temperature corresponding to maximum heat capacity, T-p, varied with scan rate. Especially with scan rates below 90 degrees C/h, T-p became strongly dependent on scan-rate, indicating that the reactions involved in the denaturation/aggregation of beta-lactoglobulin are strongly kinetically controlled. With DSC, only one peak was seen at all scan rates, but with decreasing scan rate the peak became more asymmetrical. With the low scan rate of the adiabatic experiment (approximate to 2 degrees C/h) a shoulder at ca. 60 degrees C was observed, clearly indicating that more than one process is occurring. Furthermore, the adiabatic experiment showed that the denaturation/aggregation of beta-lactoglobulin may occur within an infinitely small temperature interval, due to very slow irreversible processes. (C) 1997 Elsevier Science B.V. [References: 22]
机译：通过扫描量热法研究了牛β-乳球蛋白（50 g / l）在中性pH下的变性和聚集。为了涵盖广泛的扫描速率（2-1200摄氏度/小时），我们使用了三种不同的量热仪：两个扫描量热仪（PE DSC7和Hart Scientific DSC 4207）和绝热量热仪。对应于最大热容量T-p的温度随扫描速率而变化。尤其是当扫描速率低于90摄氏度/小时时，T-p强烈依赖于扫描速率，这表明与β-乳球蛋白变性/聚集有关的反应受到了强烈的动力学控制。使用DSC，在所有扫描速率下都只能看到一个峰，但是随着扫描速率的降低，该峰变得更加不对称。在绝热实验的低扫描速率下（大约2摄氏度/小时），肩部大约在观察到60摄氏度，清楚地表明正在发生一个以上的过程。此外，绝热实验表明，由于非常缓慢的不可逆过程，β-乳球蛋白的变性/聚集可能在无限小的温度间隔内发生。 （C）1997 Elsevier Science B.V. [参考：22]

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