Thermal denaturation analysis of super thermostable cellulase using TC-700

The thermodynamic properties and secondary structures of proteins reveal important information on their functions. Differential scanning calorimetry (DSC) and CD spectroscopy are usually used to measure the thermal denaturation of proteins. CD spectroscopy has advantages such that CD spectra can be measured using lower concentrations of proteins than DSC and can also be measured at various pHs and in a wider range of solvent conditions. However, CD spectra cannot be measured at the temperature above 100ºC because the boiling point of water is 100ºC.

Jasco has developed the TC-700/700PC type, high pressure-resistant/high temperature measurement sample chamber for high temperature measurements above 100ºC. TC-700 enables measurement of CD spectra at temperatures up to 170ºC by pressurizing the sample solution to 1 MPa using commercially available high-pressure N2 gas. Using TC-700, the thermal denaturation of super thermostable proteins, such as those originating from thermophiles, can be measured.

Herein, thermal denaturation analysis of super thermostable cellulase using TC-700PC is explained. Super thermostable cellulase maintains its activity at temperatures up to 90ºC. Research on enzymes, such as super thermostable cellulase, may lead to the development of methods for the production of bioethanol from agricultural waste rather than from important crops, such as corn or sugarcane.