The stability of recombinant Aspergillus aculeatus PME (pectin methylesterase), an enzyme with high β-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 °C. This could be correlated to the irreversible enzyme inactivation observed at that temperature. Hydrostatic pressure greater than 1 GPa was necessary to induce changes in the enzyme's secondary structure. No enzyme inactivation was observed at up to 700 MPa. Pressure increased PME stability towards thermal denaturation. At 200 MPa, temperatures above 60 °C were necessary to cause significant PME unfolding and loss of activity. These results may be relevant for an understanding of the extreme stability of amyloid fibrils for which β-helices have been proposed as a structural element.
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December 2005
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Research Article|
December 06 2005
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 β-helices
Carolien Dirix;
Carolien Dirix
1
*Department of Chemistry, Faculty of Sciences, Katholieke Universiteit Leuven, Celestijnenlaan 200 D, B-3001 Leuven, Belgium
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Thomas Duvetter;
Thomas Duvetter
1
†Centre of Food and Microbial Technology, Faculty of Applied Biosciences and Engineering, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee, Belgium
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Ann Van Loey;
Ann Van Loey
†Centre of Food and Microbial Technology, Faculty of Applied Biosciences and Engineering, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee, Belgium
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Marc Hendrickx;
Marc Hendrickx
†Centre of Food and Microbial Technology, Faculty of Applied Biosciences and Engineering, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee, Belgium
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Karel Heremans
Karel Heremans
2
*Department of Chemistry, Faculty of Sciences, Katholieke Universiteit Leuven, Celestijnenlaan 200 D, B-3001 Leuven, Belgium
2To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
May 03 2005
Revision Received:
July 19 2005
Accepted:
July 28 2005
Accepted Manuscript online:
July 28 2005
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 392 (3): 565–571.
Article history
Received:
May 03 2005
Revision Received:
July 19 2005
Accepted:
July 28 2005
Accepted Manuscript online:
July 28 2005
Citation
Carolien Dirix, Thomas Duvetter, Ann Van Loey, Marc Hendrickx, Karel Heremans; 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 β-helices. Biochem J 15 December 2005; 392 (3): 565–571. doi: https://doi.org/10.1042/BJ20050721
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