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Purification and some properties of pectinesterase from potato (Solanum tuberosum L.) alpha cultivar

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dc.creator Montañez Sáenz, Julio
dc.creator Téllez, Alejandro
dc.creator Garza, Heliodoro de la
dc.creator Reyes, María de la Luz
dc.creator Contreras-Esquivel, Juan Carlos
dc.creator Aguilar, Cristóbal Noé
dc.date 2007-11-15T15:50:16Z
dc.date 2007-11-15T15:50:16Z
dc.date 2000
dc.date.accessioned 2017-01-31T00:58:41Z
dc.date.available 2017-01-31T00:58:41Z
dc.identifier Braz. arch. biol. technol., 2000, vol.43, no.4, p.0-0
dc.identifier 1516-8913
dc.identifier http://hdl.handle.net/10261/2173
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2173
dc.description Pectinesterase was extracted from potato alpha cultivar, purified and partially characterized The used protocol resulted in a 58.8-fold purification (51 850.2 units/mg protein) with 15.5% recovery of pectinesterase activity. The purified enzyme had a molecular weight of 27 kDa and its isoelectric point was around 4.5 with pH and temperature optima of 8.0 and 60°C, respectively. The purified enzyme had a single symmetric peak of specific activity after chromatographic steps. The homogeneity of the purified pectinesterase was confirmed by gel filtration and polyacrylamide electrophoresis gel
dc.description Authors wish to thank National Council for Science & Technology (CONACYT, México 83076/124550). This research was partially supported by the CGEPI-UAdeC and forms part of the thesis work of Julio Cesar Montañez. Authors wish to thank researchers of PP-4 of Biotechnology Dept, in the Universidad Autonoma Metropolitana Iztapalapa for facilities and critical opinions offered.
dc.description Peer reviewed
dc.language eng
dc.publisher Instituto de Tecnologia do Paraná
dc.rights openAccess
dc.subject Extraction
dc.subject Purification
dc.subject Properties
dc.subject Pectinesterase
dc.subject Potato
dc.title Purification and some properties of pectinesterase from potato (Solanum tuberosum L.) alpha cultivar
dc.type Artículo


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