Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier

A 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 therm...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Afaq,Sarah, Iqbal,Jawaid
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2001
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300006
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:scielo:S0717-34582001000300006
record_format dspace
spelling oai:scielo:S0717-345820010003000062003-08-18Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrierAfaq,SarahIqbal,Jawaid A 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.4 n.3 20012001-12-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300006en
institution Scielo Chile
collection Scielo Chile
language English
description A 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.
author Afaq,Sarah
Iqbal,Jawaid
spellingShingle Afaq,Sarah
Iqbal,Jawaid
Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
author_facet Afaq,Sarah
Iqbal,Jawaid
author_sort Afaq,Sarah
title Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
title_short Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
title_full Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
title_fullStr Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
title_full_unstemmed Immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
title_sort immobilization and stabilization of papain on chelating sepharose: a metal chelate regenerable carrier
publisher Pontificia Universidad Católica de Valparaíso
publishDate 2001
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300006
work_keys_str_mv AT afaqsarah immobilizationandstabilizationofpapainonchelatingsepharoseametalchelateregenerablecarrier
AT iqbaljawaid immobilizationandstabilizationofpapainonchelatingsepharoseametalchelateregenerablecarrier
_version_ 1718441696980631552