Immobilization of pectinmethylesterase from acerola (Malpighia glabra L.) in porous silica

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorde Assis, S. A.
dc.creatorTrevisan, H. C.
dc.creatorMascarenhas, O. M.
dc.creatorOliveira, F.
dc.date2014-05-20T15:20:39Z
dc.date2016-10-25T17:53:49Z
dc.date2014-05-20T15:20:39Z
dc.date2016-10-25T17:53:49Z
dc.date2003-06-01
dc.date.accessioned2017-04-05T23:26:58Z
dc.date.available2017-04-05T23:26:58Z
dc.identifierBiotechnology Letters. Dordrecht: Kluwer Academic Publ, v. 25, n. 11, p. 869-872, 2003.
dc.identifier0141-5492
dc.identifierhttp://hdl.handle.net/11449/31907
dc.identifierhttp://acervodigital.unesp.br/handle/11449/31907
dc.identifier10.1023/A:1024088326346
dc.identifierWOS:000183320800007
dc.identifierhttp://dx.doi.org/10.1023/A:1024088326346
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/876353
dc.descriptionThe total and partially purified enzyme pectinmethylesterase from acerola fruit was covalently immobilized on porous silica particles. These efficiency values were 114% for the total PME and 351% for the partially purified PME. In both forms the immobilization resulted in compounds with high thermal stability.
dc.languageeng
dc.publisherKluwer Academic Publ
dc.relationBiotechnology Letters
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectacerola
dc.subjectimmobilization
dc.subjectkinetic characterization
dc.subjectpectinmethylesterase
dc.subjectpurification
dc.titleImmobilization of pectinmethylesterase from acerola (Malpighia glabra L.) in porous silica
dc.typeOtro


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