Abstract
The effect of hydration andpH on the thermal stability of proteinase K was studied in the temperature range 310–450 K by differential scanning calorimetry. The dependences of the denaturation temperatureT d, the specific enthalpy of denaturation ΔH d and the maximum of excess apparent specific heat capacityC maxex upon the degree of hydrationh and thepH of the buffers used are presented. The relation betweenT d andh is of the Flory-Garrett's type. By means of Ooi's model, the two components of the denaturation enthalpy arising from hydration and conformational change, respectively, were estimated. The fact that the specific denaturation enthalpy of proteinase K is very low may be attributed to its very low enthalpy of conformational change per heavy atom.
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Dedicated to Prof. Menachem Steinberg on the occasion of his 65th birthday
This major project was supported by the National Natural Science Foundation of China.
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Bangning, W., Buxing, H. & Fu, T. Effect of hydration andpH on the thermal stability of proteinase K. Journal of Thermal Analysis 50, 73–80 (1997). https://doi.org/10.1007/BF01979550
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DOI: https://doi.org/10.1007/BF01979550