Thermal Inactivation of Pectinesterase in Papaya Pulp (pH 3.8)

Massaguer, Pilar Rodriguez de; Magalhães, Matheus Albergaria de; Tosello, R.M.

doi:10.1007/978-1-4615-2674-2_158

Cited by 7 publications

(5 citation statements)

References 2 publications

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“…This value is somewhat lower than those obtained by Van den Broeck et al (67) (301.4-350.5 kJ/mol) for commercial orange PME. Massaguer et al (72) also reported activation energy levels of 61.7 kcal/mol (257.9 kJ/mol) and 72.7 kcal/mol (303.9 kJ/mol) for the thermal inactivation of heatlabile and heat-stable PME from acidified papaya pulp.…”

Section: Resultsmentioning

confidence: 89%

Partial Purification, Characterization, and Thermal and High-Pressure Inactivation of Pectin Methylesterase from Carrots (DaucuscarrotaL.)

Nguyen

Loey

Fachin

et al. 2002

J. Agric. Food Chem.

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Pectin methylesterase (PME) from carrots (Daucus carrota L.) was extracted and purified by affinity chromatography on a CNBr-Sepharose 4B-PME inhibitor column. A single protein and PME activity peak was obtained. A biochemical characterization in terms of molar mass (MM), isoelectric points (pI), and kinetic parameters of carrot PME was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal and combined isothermal-isobaric inactivation of purified carrot PME could be described by a fractional-conversion model.

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Section: Resultsmentioning

confidence: 89%

Partial Purification, Characterization, and Thermal and High-Pressure Inactivation of Pectin Methylesterase from Carrots (DaucuscarrotaL.)

Nguyen

Loey

Fachin

et al. 2002

J. Agric. Food Chem.

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“…The thermal inactivation of PME in various fruit and vegetable model systems has been the object of many accounts in the scientific literature, very often in terms of D (decimation time) and z (∆T corresponding to a 90% decrease of D) parameters. The data obtained by various authors (27,(31)(32)(33)(34)(35) were compared, and all the obtained values of the inactivation rate constant k reported along with our measurements on the same Arrhenius plot (data not shown). Despite widely different model systems and treatment conditions, it clearly appears that the inactivation rate of PME is more heat-sensitive at lower temperatures.…”

Section: Resultsmentioning

confidence: 95%

Tomato (Lycopersicon esculentum) Pectin Methylesterase and Polygalacturonase Behaviors Regarding Heat- and Pressure-Induced Inactivation

Crelier

Robert

Claude

et al. 2001

J. Agric. Food Chem.

116

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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.

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“…This value is slightly higher than those obtained by Van den Broeck et al (1999a) (301.4 to 350.5 kJ/mol) for com- mercial orange PME. Massaguer et al (1994) reported activation energy levels of 61.7 kcal/mol (257.9 kJ/mol) and 72.7 kcal/mol (303.9 kJ/mol) for the thermal inactivation of heat-labile and heat-stable PME from acidi-®ed papaya pulp.…”

Section: Thermal Inactivation Kinetics Of Puri®ed Banana Pmementioning

confidence: 99%

Purification, characterization, thermal, and high‐pressure inactivation of pectin methylesterase from bananas (cv Cavendish)

Nguyen

Loey

Fachin

et al. 2002

Biotech & Bioengineering

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Pectin methylesterase (PME) was extracted from bananas (cv Cavendish) and purified by affinity chromatography on a CNBr-Sepharose-PME inhibitor (PMEI) column. A single protein and PME activity peak was obtained. For banana PME, a biochemical characterization in terms of molar mass (MM), pI, and kinetic parameters was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal inactivation of purified banana PME could be described by a first-order kinetic model in a temperature range of 65 degrees to 72.5 degrees C, whereas its isobaric-isothermal inactivation followed a fractional-conversion model. Banana PME was found to be more thermally stable compared with PMEs extracted from orange, tomato, and apple.

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Thermal Inactivation of Pectinesterase in Papaya Pulp (pH 3.8)

Cited by 7 publications

References 2 publications

Partial Purification, Characterization, and Thermal and High-Pressure Inactivation of Pectin Methylesterase from Carrots (DaucuscarrotaL.)

Partial Purification, Characterization, and Thermal and High-Pressure Inactivation of Pectin Methylesterase from Carrots (DaucuscarrotaL.)

Tomato (Lycopersicon esculentum) Pectin Methylesterase and Polygalacturonase Behaviors Regarding Heat- and Pressure-Induced Inactivation

Purification, characterization, thermal, and high‐pressure inactivation of pectin methylesterase from bananas (cv Cavendish)

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