Enzyme and microbial technology vol:36 issue:4 pages:385-390
The thermal inactivation kinetics of purified Aspergillus aculeatus pectin methylesterase (PME) was investigated. In the temperature range 46-56 degreesC A. aculeatus PME inactivates following a first-order reaction. Addition of CaCl2 (50 mM or 1.0 M) has no noticeable influence Oil the inactivation parameters. A. aculeatus PME is very pressure stable, at 25 degreesC no loss of activity was noticed after pressurization at 700 MPa for I 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. (C) 2004 Elsevier Inc. All rights reserved.