Mild‐Heat and High‐Pressure Inactivation of Carrot Pectin Methylesterase: A Kinetic Study

Nguyen, Binh Ly; Loey, Ann M. Van; Smout, Chantal; ErenÖzcan, S.; Fachin, D.; Verlent, I.; Truong, Sharon; Duvetter, Thomas; Hendrickx, Marc

doi:10.1111/j.1365-2621.2003.tb09653.x

Cited by 100 publications

(69 citation statements)

References 27 publications

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“…Another possible source of the high pressure stability may be the presence of ß-helices in amyloid fibrils. It is well known that enzymes that contain ß-helices are very pressure stable (59).…”

Section: Intermolecular Interactions Of Unfolded Proteinsmentioning

confidence: 99%

Protein dynamics: hydration and cavities

Heremans

2005

Braz J Med Biol Res

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The temperature-pressure behavior of proteins seems to be unique among the biological macromolecules. Thermodynamic as well as kinetic data show the typical elliptical stability diagram. This may be extended by assuming that the unfolded state gives rise to volume and enthalpy-driven liquid-liquid transitions. A molecular interpretation follows from the temperature and the pressure dependence of the hydration and cavities. We suggest that positron annihilation spectroscopy can provide additional quantitative evidence for the contributions of cavities to the dynamics of proteins. Only mature amyloid fibrils that form from unfolded proteins are very resistant to pressure treatment.

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Section: Intermolecular Interactions Of Unfolded Proteinsmentioning

confidence: 99%

Protein dynamics: hydration and cavities

Heremans

2005

Braz J Med Biol Res

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“…However, PME enzymes have been found that exhibit a wide thermal stability range in orange, acerola and carrot juices. This suggests the presence of thermostable and thermolabile fractions of PME isoenzyme complexes with irregular characteristics (Arbaisah et al, 1996;de Assis et al, 2000;Ly-Nguyen et al, 2003;Versteeg et al, 1980). In this regard, it should be noted that the technological problems in citrus juice associated with PME have been attributed to a high molecular weight thermostable fraction, which is also crucial in the establishment of pasteurization values in orange juice (Versteeg et al, 1980).…”

Section: Introductionmentioning

confidence: 99%

Thermal inactivation kinetics of partially purified mango pectin methylesterase

et al. 2016

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Kinetic parameters of thermal inactivation of pectin methylesterase (PME) in a partially purified mango enzyme extract were determined. The PME of mango partially purified by salting out showed different patterns of thermal inactivation, indicating the presence of a thermostable fraction at 70 °C and a thermolabile fraction at lower temperatures. The inactivation of the thermostable fraction exhibited a linear behavior that yielded a z-value of 9.44 °C and an activation energy (Ea) of 245.6 kJ mol -1 K -1 using the Arrhenius model. The thermostable mango PME fraction represented 17% of total crude enzyme extract, which emphasizes the importance of residual enzyme activity after heat treatment.

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“…La desnaturalización de enzimas por calor, suele a menudo ser irreversible debido a la ruptura de enlaces covalentes y/o la agregación de proteínas desdobladas (Ly-Nguyen et al, 2003;Puppo et al, 2004).…”

Section: Determinación De La Concentración De Proteínasunclassified

Inactivación Térmica de Pectinmetilesterasa en Tomate de Árbol (Solanum betaceum)

2013

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* Autor a quien debe ser dirigida la correspondenciaRecibido Nov. 22, 2012; Aceptado Ene. 08, 2013; Versión final recibida Mar. 05, 2013 Resumen El objetivo de esta investigación fue estudiar el efecto del procesamiento térmico a temperatura constante, sobre la actividad residual de la enzima pectinmetilesterasa (PME), causante de la separación de fases en néctar de tomate de árbol (Solanum betaceum). Se evaluó un rango de temperaturas entre 40 y 90°C y tiempos de exposición entre los 5 y 20s. La actividad enzimática residual se midió por espectrofotometría a una longitud de onda de 620 nm. Se determinó el contenido de proteína mediante el método de Bradford. El tratamiento térmico aplicado a 60ºC durante 20 segundos de exposición redujo la actividad residual de PME hasta un 10% evitando la separación de fases del néctar. Se concluye que el tratamiento aplicado disminuyó el contenido de enzima en un 28% con respecto al testigo sin tratar. Palabras clave: actividad residual, pectinmetilesterasa, tomate de árbol, tratamiento térmico, inactivación térmica Thermal Inactivation of Pectinmethylesterase in Tree Tomato (Solanum betaceum) AbstractThe effect of batch thermal processing on the residual activity of pectinmethylesterase enzyme (PME) in tree tomato (Solanum betaceum) was studied. Batch processes were conducted at temperatures between 40 and 90°C and exposure times from 5 to 20s. Residual enzyme activity was spectrophotometrically measured at 620 nm wavelength. The protein content was determined according to Bradford´s dye binding method. The thermal treatment applied to 60°C for 20 seconds exposure time, reduced the residual activity of PME to 10% avoiding phase separation. It is concluded that the thermal treatment applied caused a decrease on enzyme content to 28% from initial content.

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Mild‐Heat and High‐Pressure Inactivation of Carrot Pectin Methylesterase: A Kinetic Study

Cited by 100 publications

References 27 publications

Protein dynamics: hydration and cavities

Protein dynamics: hydration and cavities

Thermal inactivation kinetics of partially purified mango pectin methylesterase

Inactivación Térmica de Pectinmetilesterasa en Tomate de Árbol (Solanum betaceum)

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