Tomato (Lycopersicon esculentum) pectin methylesterase and polygalacturonase behaviors regarding heat- and pressure-induced inactivation.
The combined high pressure/thermal (HP/T) inactivation of tomato pectin methyl esterase (PME) and polygalacturonase (PG) was investigated as a possible alternative to thermal processing classically used for enzyme inactivation. The temperature and pressure ranges tested were from 60 degrees C to 105 degrees C, and from 0.1 to 800 MPa, respectively. PME, a heat-labile enzyme at ambient pressure, is dramatically stabilized against thermal denaturation at pressures above atmospheric and up to 500-600 MPa. PG, however, is very resistant to thermal denaturation at 0.1 MPa, but quickly and easily inactivated by combinations of moderate temperatures and pressures. Selective inactivation of either PME or PG was achieved by choosing proper combinations of P and T. The inactivation kinetics of these enzymes was measured and described mathematically over the investigated portion of the P/T plane. Whereas medium composition and salinity had little influence on the inactivation rates, PME was found less sensitive to both heat and pressure when pH was raised above its physiological value. PG, on the other hand, became more labile at higher pH values. The results are discussed in terms of isoenzymes and other physicochemical features of PME and PG.
Crelier
S
S
Nestlé PTC-Kemptthal, 8310 Kemptthal, Switzerland. simon.crelier@rdke.nestle.com
Robert
M C
MC
Claude
J
J
Juillerat
M A
MA
D019149:Bioreactors; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006358:Hot Temperature; D018551:Solanum lycopersicum / Q000201:enzymology*; D011096:Polygalacturonase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011312:Pressure
D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase; D011096:Polygalacturonase