Brasil | Otro
dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorBonine, Barbara Martineli
dc.creatorPolizelli, Patricia Peres
dc.creatorBonilla-Rodriguez, Gustavo Orlando
dc.date2015-04-27T11:55:52Z
dc.date2016-10-25T20:46:36Z
dc.date2015-04-27T11:55:52Z
dc.date2016-10-25T20:46:36Z
dc.date2014
dc.date.accessioned2017-04-06T08:08:20Z
dc.date.available2017-04-06T08:08:20Z
dc.identifierEnzyme Research, v. 2014, p. 1-7, 2014.
dc.identifier2090-0406
dc.identifierhttp://hdl.handle.net/11449/122576
dc.identifierhttp://acervodigital.unesp.br/handle/11449/122576
dc.identifierhttp://dx.doi.org/10.1155/2014/738739
dc.identifierISSN2090-0406-2014-2014-01-07.pdf
dc.identifier6955258588672130
dc.identifierhttp://www.hindawi.com/journals/er/2014/738739/
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/933197
dc.descriptionThis study reports the immobilization of a new lipase isolated from oleaginous seeds of Pachira aquatica, using beads of calcium alginate (Alg) and poly(vinyl alcohol) (PVA). We evaluated the morphology, number of cycles of reuse, optimum temperature, and temperature stability of both immobilization methods compared to the free enzyme. The immobilized enzymes were more stable than the free enzyme, keeping 60% of the original activity after 4 h at 50°C. The immobilized lipase was reused several times, with activity decreasing to approximately 50% after 5 cycles. Both the free and immobilized enzymes were found to be optimally active between 30 and 40°C.
dc.languageeng
dc.relationEnzyme Research
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleImmobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
dc.typeOtro


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