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dc.creatorAfaq,Sarah
dc.creatorIqbal,Jawaid
dc.date2001-12-01
dc.date.accessioned2019-05-03T12:43:59Z
dc.date.available2019-05-03T12:43:59Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300006
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/84684
dc.descriptionA method for immobilization of papain has been selected based on the interaction between its histidine, cysteine and tryptophan residues with the immobilized metal ion (IMI) carrier for maximum binding on a small volume of the carrier. The immobilized papain retained high activity has improved thermal stability and the carrier could be recovered from the spent bound enzyme, to be reused. Reimmobilization of papain on the regenerated matrix was equally effective with the retention of maximum enzyme activity.
dc.formattext/html
dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.relation10.4067/S0717-34582001000300006
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.4 n.3 2001
dc.titleImmobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier


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