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Updated: Apr 19, 2026
Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
Enhancing the thermal stability of inulin fructotransferase with high hydrostatic pressure
Yungao Li1, Ming Miao1, Miao Liu1
1State Key Laboratory of Food Science and Technology, Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, Jiangsu 214122, PR China.
Abstract:
The thermal stability of inulin fructotransferase (IFTase) subjected to high hydrostatic pressure (HHP) was studied. The value of inactivation rate of IFTase in the range of 70-80°C decreased under the pressure of 100 or 200 MPa, indicating that the thermostability of IFTase under high temperature was enhanced by HHP. Far-UV CD and fluorescence spectra showed that HHP impeded the unfolding of the conformation of IFTase under high temperature, reflecting the antagonistic effect between temperature and pressure on IFTase. The new intramolecular disulfide bonds in IFTase were formed under a combination of HHP and high temperature. These bonds might be related to the stabilization of IFTase at high temperature. All the above results suggested that HHP had the protective effect on IFTase against high temperature.
