Article ID Journal Published Year Pages File Type
10233217 Enzyme and Microbial Technology 2005 6 Pages PDF
Abstract
The thermal inactivation kinetics of purified Aspergillus aculeatus pectin methylesterase (PME) was investigated. In the temperature range 46-56 °C A. aculeatus PME inactivates following a first-order reaction. Addition of CaCl2 (50 mM or 1.0 M) has no noticeable influence on the inactivation parameters. A. aculeatus PME is very pressure stable, at 25 °C no loss of activity was noticed after pressurization at 700 MPa for 1 h. Pressure and temperature exhibit an antagonistic effect on the enzyme stability. Furthermore A. aculeatus PME was unsusceptible for inhibition by PME inhibitor purified from kiwi.
Related Topics
Physical Sciences and Engineering Chemical Engineering Bioengineering
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