Abstract
The influence of polyhydric alcohols (sorbitol, xylitol, erythritol, glycerol) on the thermal stability of Rhizomucor miehei lipase has been studied at high hydrostatic pressure (up to 500 MPa). In the absence of additives, a protective effect (PE) (the ratio between the residual activities determined at 480 MPa for the enzyme in the presence or absence of polyhydric alcohols) of low-applied pressures (from 50 MPa to 350 MPa) against thermal deactivations (at 50°C and 55°C) has been noticed. In the presence of additives, a strong correlation between PE and the total hydroxyl group concentration has been obtained, for the first time, under treatments of combining denaturing temperatures and high hydrostatic pressures. This relationship does not seem to be dependent on the nature polyhydric alcohols as the same effect could be observed with 1 M sorbitol and 2 M glycerol. This PE, against thermal and high pressure combined lipase deactivation, increases with polyhydric alcohol concentrations, and when temperature increases from 25°C to 55°C.
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Abbreviations
- C n :
-
n carbon atoms
- kDa:
-
Molecular weight unit (103Â Da)
- M:
-
Molar concentration unit (mol.l−1)
- MPa:
-
Pressure unit (106Â P=10Â bars)
- OH group:
-
Hydroxyl group
- PE:
-
Protective effect
- PME:
-
Pectin methylesterase
- P50% :
-
Pressure of half deactivation for a settled treatment time (MPa)
- RML:
-
Rhizomucor miehei lipase
- t 1/2 :
-
Half-life (min)
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Acknowledgments
Marilyne Noël (pHD student) and authors are very grateful to Peter Winterton for improving the English of the manuscript.
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Noël, M., Lozano, P. & Combes, D. Polyhydric alcohol protective effect on Rhizomucor miehei lipase deactivation enhanced by pressure and temperature treatment. Bioprocess Biosyst Eng 27, 375–380 (2005). https://doi.org/10.1007/s00449-005-0417-1
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DOI: https://doi.org/10.1007/s00449-005-0417-1