Effects of temperature and pressure on Rhizomucor miehei lipase stability
作者： Marilyne Noel , Didier Combes
DOI: 10.1016/S0168-1656(02)00359-0
关键词:
摘要: Both high temperature and hydrostatic pressure induce irreversible deactivation of enzymes. They enable the enzyme's thermodynamic parameters to be determined are used study mechanisms involved in biochemical systems. The effect these two factors on stability Rhizomucor miehei lipase have been investigated. criterion was residual hydrolytic activity lipase. Experimental theoretical parameters, obtained by linear regression analysis, were compared with kinetics order validate series-type inactivation model. R. deactivated either thermal or treatment. Moreover conformational studies made fluorescence spectroscopy suggest that changes induced different from those temperature. In addition they show after there less intermolecular hydrogen bonded structures formed than case for pressure.
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