Extraction, thermal stability and kinetic behavior of pectinmethylesterase from hawthorn (Crataegus pubescens) fruit

Vivar-Vera, M. A.; Salazar-Montoya, Juan Alfredo; Calva-Calva, Graciano; Ramos-Ramírez, Emma Gloria

doi:10.1016/j.lwt.2005.10.005

Cited by 21 publications

(10 citation statements)

References 34 publications

(24 reference statements)

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“…Activation energy obtained (105.7 kJ mol À1 ) was similar to that obtained for heat inactivation of soybean trypsin inhibitors, from 103 to 195 kJ mol À1 depending on the product moisture (van den Hout et al, 1999). Comparable values, 102.3 kJ mol À1 and 146 kJ mol À1 , were observed for adenosine deaminase (Alrokayan, 2002) and pectinmethylesterase (Vivar-Vera et al, 2007) from skeletal muscle and hawthorn, respectively. Table 2 also shows thermodynamic values (DH * , DG * and DS * ) obtained from Eq.…”

Section: Resultssupporting

confidence: 73%

Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A

Lappe

Cladera-Olivera

Dominguez

et al. 2009

Journal of Food Engineering

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Section: Resultssupporting

confidence: 73%

Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A

Lappe

Cladera-Olivera

Dominguez

et al. 2009

Journal of Food Engineering

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“…Karakus and Pekyardimci (2012) reported temperature optimum of free PME from Malatya apricot as 60°C which is in accord the one found in this study. Reported temperature optima for PMEs from different sources include 55°C for black carrot (Unal and Bellur 2009), 55°C for hawthorn (Vivar-Vera et al 2007), between 52.5 and 55.0 for green pepper (Castro et al 2004), 55°C for tomato (Van Den Broeck et al 2000), 65°C for plum (Prunus domestica) (Nunes et al 2006), which are similar to the one obtained in this study. However, higher temperature optima were reported for PME from guava, e.g.…”

Section: Resultssupporting

confidence: 83%

“…In a study carried out by Karakus and Pekyardimci (2012) on comparison of covalent and noncovalent immobilization of pectinesterase isolated from Malatya apricot, it was found that the pH optima of covalently-immobilized and free PME were 8.0 and 9.0, respectively, which is slightly higher than the one found for Alyanak PME. Some of the reported optimum pH values for PME from different sources are 7.5 for black carrot (Daucus carota L.) (Unal and Bellur 2009), green pepper (Castro et al 2004), plum (Nunes et al 2006) and hawthorn (Vivar-Vera et al 2007), 8.0 for orange (Amaral et al 2005), 8.0 for peach (Javeri and Wicker 1991), 9.0 for guava (Carvalho et al 2009). The pH optimum of 7.5 found in this study was in accord with these values.…”

Section: Resultsmentioning

confidence: 99%

“…PMEs are cell wall-bound enzymes which catalyze the hydrolytic cleavage of the methylester moieties on pectin molecules, resulting in the release of methanol and partially de-esterified pectin (Unal and Bellur 2009). The control of PME activity has been a common subject of study because of the implications in the modification of the texture of fruit and vegetables and as a destabilizing agent of pectin materials in fruit juices and concentrates (Balogh et al 2004;Vivar-Vera et al 2007;Gupta et al 2011).…”

Section: Introductionmentioning

confidence: 99%

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Extraction and characterization of pectin methylesterase from Alyanak apricot (Prunus armeniaca L)

Ünal

Şener

2013

J Food Sci Technol

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This study was carried out to determine some of the biochemical properties of pectin methylesterase (PME) from Alyanak apricot which is an important variety grown in Malatya region of Turkey. The enzyme had high activity in a pH range of 7.0-8.0 with the maximal activity occurring at pH 7.5. However, the enzyme activity at high and low pH values was very low. The optimum temperature for maximal PME activity was found to be 60°C. The activity of PME has been enhanced by NaCl, particularly at 0.15 M. K m and V max values for Alyanak apricot PME using apple pectin as substrate were found to be 1.69 mg/mL (r 2 =0.992) and 3.41 units/mL, respectively. The enzyme was stable at 30-45°C/10 min whereas it lost nearly all of its activity at 80°C/10 min. E a and Z values were found to be 206.1 kJ/mol (r 2 =0.993) and 10.62°C (r 2 =0.992), respectively.

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“…En otros jugos de frutas, como la naranja, se ha recomendado ajustar las condiciones de tratamiento térmico para reducir la actividad de PME (Giner et al, 2000). También se encuentran estudios en maracuyá (Vivar-Vera et al, 2007), fresa (Osorio et al, 2008) y frambuesa (Jakób et al, 2009) entre otras. El objetivo de esta investigación fue inactivar parcialmente la enzima PME, causante de la separación de fases en el zumo de tomate de árbol.…”

Section: Introductionunclassified

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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Extraction, thermal stability and kinetic behavior of pectinmethylesterase from hawthorn (Crataegus pubescens) fruit

Cited by 21 publications

References 34 publications

Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A

Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A

Extraction and characterization of pectin methylesterase from Alyanak apricot (Prunus armeniaca L)

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

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