The in situ observation of the temperature and pressure stability of recombinant Aspergillus aculeatus pectin methylesterase with Fourier transform IR spectroscopy reveals an unusual pressure stability of beta-helices.

@article{Dirix2005TheIS,
  title={The in situ observation of the temperature and pressure stability of recombinant Aspergillus aculeatus pectin methylesterase with Fourier transform IR spectroscopy reveals an unusual pressure stability of beta-helices.},
  author={Carolien Dirix and Thomas Duvetter and Ann M. Van Loey and Marc Van Hendrickx and Karel Heremans},
  journal={The Biochemical journal},
  year={2005},
  volume={392 Pt 3},
  pages={565-71}
}
The stability of recombinant Aspergillus aculeatus PME (pectin methylesterase), an enzyme with high beta-helix content, was studied as a function of pressure and temperature. The conformational stability was monitored using FTIR (Fourier transform IR) spectroscopy whereas the functional enzyme stability was monitored by inactivation studies. Protein unfolding followed by amorphous aggregation, which makes the process irreversible, was observed at temperatures above 50 degrees C. This could be… CONTINUE READING