Please use this identifier to cite or link to this item: http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2173
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dc.creatorMontañez Sáenz, Julio-
dc.creatorTéllez, Alejandro-
dc.creatorGarza, Heliodoro de la-
dc.creatorReyes, María de la Luz-
dc.creatorContreras-Esquivel, Juan Carlos-
dc.creatorAguilar, Cristóbal Noé-
dc.date2007-11-15T15:50:16Z-
dc.date2007-11-15T15:50:16Z-
dc.date2000-
dc.date.accessioned2017-01-31T00:58:41Z-
dc.date.available2017-01-31T00:58:41Z-
dc.identifierBraz. arch. biol. technol., 2000, vol.43, no.4, p.0-0-
dc.identifier1516-8913-
dc.identifierhttp://hdl.handle.net/10261/2173-
dc.identifier.urihttp://dspace.mediu.edu.my:8181/xmlui/handle/10261/2173-
dc.descriptionPectinesterase 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.descriptionAuthors 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.descriptionPeer reviewed-
dc.languageeng-
dc.publisherInstituto de Tecnologia do Paraná-
dc.rightsopenAccess-
dc.subjectExtraction-
dc.subjectPurification-
dc.subjectProperties-
dc.subjectPectinesterase-
dc.subjectPotato-
dc.titlePurification and some properties of pectinesterase from potato (Solanum tuberosum L.) alpha cultivar-
dc.typeArtículo-
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