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Optimization, Heat Stability and Kinetic Characterization of Pectin- Methylesterase Enzyme from Tomato (Solanum lycopersicum ‘Zinac’) Fruits

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dc.contributor.authorPinheiro, Joaquina
dc.contributor.authorSilva, Cristina L. M.
dc.contributor.authorAlegria, C.
dc.contributor.authorAbreu, Marta
dc.contributor.authorGonçalves, Elsa M.
dc.date.accessioned2013-01-28T19:31:39Z
dc.date.available2013-01-28T19:31:39Z
dc.date.issued2012
dc.description.abstractTextural changes during fruit ripening have been attributed to pectin degradation due to pectic enzymes such as pectinmethylesterase (PME, EC 3.1.1.11). PME catalyzes the de-esterification of pectin, a complex mixture of polysaccharides, namely methyl esterified polygalacturonic acid, with the release of hydrogen and methanol, producing shorter chains causing drastic losses in firmness. Thus, control of PME activity in fruits aiming at texture maintenance and/or improvement is extremely important to the food industry. However, PME activity and properties are dependent on product, environmental and physico-chemical conditions, such as pH and temperature. Therefore, the aim of the present work was to optimize the pectinmethylesterase (PME) enzyme assay from tomato (Solanum lycopersicum ‘Zinac’) fruits, and determine its kinetics behavior and thermal stability. The highest PME activity was found with a 1.0 M of NaCl extraction solution, with 0.5% citrus pectin, and revealed optima of temperature at 60°C and pH of 8.8. The low kM value (0.011%) for tomato PME describes the high affinity between enzyme and substrate (citrus pectin), whereas the obtained Vmax value (0.712 U mg-1) relates to the enzyme quantity present in the reaction. The study of PME thermal stability showed two distinct behaviors: an increase of activity from 40 to 50°C and a decrease from 55 to 80°C. At 50°C/10 min an increase in activity up to 17% of activity was observed. At 60°C, about 50% of the activity still remained after heating for 25 min, and PME was completely inactivated at 80°C after 10 min. Data obtained in the temperature range of 55 to 80°C were also satisfactorily described by an Arrhenius first-order kinetic model. These results provide useful information about the different factors that affect tomato PME activity and may be used as a tool for firmness control during postharvest handling and fruit processing.por
dc.identifier.citationPINHEIRO, J. ...[et al.] - Optimization, Heat Stability and Kinetic Characterization of Pectin- Methylesterase Enzyme from Tomato (Solanum lycopersicum ‘Zinac’) Fruits. In XXVIII International Horticultural Congress on Science and Horticulture for People (IHC2010): International Symposium on Postharvest Technology in the Global Market, Lisboa, Portugal, 22-27 August, 2010 - ISHS Acta Horticulturae. ISSN 0567-7572. N.º 934 (2012), p. 1283-1290por
dc.identifier.urihttp://hdl.handle.net/10400.14/10034
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherInternational Society for Horticultural Sciencepor
dc.subjectpHpor
dc.subjectTemperaturepor
dc.subjectNaCl concentrationpor
dc.subjectHeat stabilitypor
dc.subjectQualitypor
dc.titleOptimization, Heat Stability and Kinetic Characterization of Pectin- Methylesterase Enzyme from Tomato (Solanum lycopersicum ‘Zinac’) Fruitspor
dc.typeconference object
dspace.entity.typePublication
person.familyNamePinheiro
person.familyNameSilva
person.familyNameAlegria
person.familyNameAbreu
person.familyNameGonçalves
person.givenNameJoaquina
person.givenNameCristina
person.givenNameCarla
person.givenNameMarta
person.givenNameElsa Margarida
person.identifier556456
person.identifier1473674
person.identifierM-8770-2015
person.identifier.ciencia-idB113-2D80-406B
person.identifier.ciencia-id6611-634A-132C
person.identifier.ciencia-id5115-6CF2-C01A
person.identifier.ciencia-idA31F-D2A3-36A8
person.identifier.ciencia-idAA12-42D6-6D59
person.identifier.orcid0000-0001-9319-2651
person.identifier.orcid0000-0002-0495-3955
person.identifier.orcid0000-0002-9461-4569
person.identifier.orcid0000-0002-0245-7122
person.identifier.orcid0000-0002-5814-0490
person.identifier.ridA-3568-2013
person.identifier.ridN-4198-2013
person.identifier.scopus-author-id25228814000
person.identifier.scopus-author-id7201387397
person.identifier.scopus-author-id25228203500
person.identifier.scopus-author-id7102768632
person.identifier.scopus-author-id7004990784
rcaap.rightsrestrictedAccesspor
rcaap.typeconferenceObjectpor
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