Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate

Detalhes bibliográficos
Autor(a) principal: Garg,N.
Data de Publicação: 2008
Outros Autores: Kumar,A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Chemical Engineering
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322008000200002
Resumo: Starch phosphorylase has been isolated from cabbage (Elephantopus scabar) leaves and partially purified using ammonium sulfate fractionation. The partially purified enzyme was desalted using Sephadex-G-25 chromatography. In the direction of polysaccharide synthesis, the enzyme showed optimum activity at pH 6.0 with two half pH optima at pH 5.3 and pH 7.1 whereas in the direction of glucose-1-phosphate formation, it showed optimum pH at pH 7.0 with half pH-optima at pH 6.4 and 7.6. The optimum temperature for the enzyme activity has been found to be 37ºC with two half temperature optima at 34ºC and 40ºC. The partially purified enzyme has been immobilized using egg shell as solid support. The percentage retention of the enzyme on egg shell was nearly 56%. After immobilization, specific activity of the enzyme increased from 0. 0225 to 0.0452. Upon immobilization, there was a slight alkaline shift in the optimum pH when assayed in both the directions. The immobilized enzyme also displayed increased optimum temperature and thermo-stability and could be reused number of times. The increase in thermo-stability and reusability of the immobilized enzyme has been exploited for the production of glucose-1-phosphate, a cytostatic compound used in cardio-therapy. The glucose-1-phosphate produced has been purified with nearly 95% purity after adsorption chromatography on norite and ion exchange chromatography on DEAE cellulose.
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spelling Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphateStarch phosphorylaseImmobilizationGlucose-1-phosphateEgg shellCabbageStarch phosphorylase has been isolated from cabbage (Elephantopus scabar) leaves and partially purified using ammonium sulfate fractionation. The partially purified enzyme was desalted using Sephadex-G-25 chromatography. In the direction of polysaccharide synthesis, the enzyme showed optimum activity at pH 6.0 with two half pH optima at pH 5.3 and pH 7.1 whereas in the direction of glucose-1-phosphate formation, it showed optimum pH at pH 7.0 with half pH-optima at pH 6.4 and 7.6. The optimum temperature for the enzyme activity has been found to be 37ºC with two half temperature optima at 34ºC and 40ºC. The partially purified enzyme has been immobilized using egg shell as solid support. The percentage retention of the enzyme on egg shell was nearly 56%. After immobilization, specific activity of the enzyme increased from 0. 0225 to 0.0452. Upon immobilization, there was a slight alkaline shift in the optimum pH when assayed in both the directions. The immobilized enzyme also displayed increased optimum temperature and thermo-stability and could be reused number of times. The increase in thermo-stability and reusability of the immobilized enzyme has been exploited for the production of glucose-1-phosphate, a cytostatic compound used in cardio-therapy. The glucose-1-phosphate produced has been purified with nearly 95% purity after adsorption chromatography on norite and ion exchange chromatography on DEAE cellulose.Brazilian Society of Chemical Engineering2008-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322008000200002Brazilian Journal of Chemical Engineering v.25 n.2 2008reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322008000200002info:eu-repo/semantics/openAccessGarg,N.Kumar,A.eng2008-07-03T00:00:00Zoai:scielo:S0104-66322008000200002Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2008-07-03T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
title Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
spellingShingle Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
Garg,N.
Starch phosphorylase
Immobilization
Glucose-1-phosphate
Egg shell
Cabbage
title_short Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
title_full Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
title_fullStr Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
title_full_unstemmed Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
title_sort Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate
author Garg,N.
author_facet Garg,N.
Kumar,A.
author_role author
author2 Kumar,A.
author2_role author
dc.contributor.author.fl_str_mv Garg,N.
Kumar,A.
dc.subject.por.fl_str_mv Starch phosphorylase
Immobilization
Glucose-1-phosphate
Egg shell
Cabbage
topic Starch phosphorylase
Immobilization
Glucose-1-phosphate
Egg shell
Cabbage
description Starch phosphorylase has been isolated from cabbage (Elephantopus scabar) leaves and partially purified using ammonium sulfate fractionation. The partially purified enzyme was desalted using Sephadex-G-25 chromatography. In the direction of polysaccharide synthesis, the enzyme showed optimum activity at pH 6.0 with two half pH optima at pH 5.3 and pH 7.1 whereas in the direction of glucose-1-phosphate formation, it showed optimum pH at pH 7.0 with half pH-optima at pH 6.4 and 7.6. The optimum temperature for the enzyme activity has been found to be 37ºC with two half temperature optima at 34ºC and 40ºC. The partially purified enzyme has been immobilized using egg shell as solid support. The percentage retention of the enzyme on egg shell was nearly 56%. After immobilization, specific activity of the enzyme increased from 0. 0225 to 0.0452. Upon immobilization, there was a slight alkaline shift in the optimum pH when assayed in both the directions. The immobilized enzyme also displayed increased optimum temperature and thermo-stability and could be reused number of times. The increase in thermo-stability and reusability of the immobilized enzyme has been exploited for the production of glucose-1-phosphate, a cytostatic compound used in cardio-therapy. The glucose-1-phosphate produced has been purified with nearly 95% purity after adsorption chromatography on norite and ion exchange chromatography on DEAE cellulose.
publishDate 2008
dc.date.none.fl_str_mv 2008-06-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322008000200002
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322008000200002
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0104-66322008000200002
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
dc.source.none.fl_str_mv Brazilian Journal of Chemical Engineering v.25 n.2 2008
reponame:Brazilian Journal of Chemical Engineering
instname:Associação Brasileira de Engenharia Química (ABEQ)
instacron:ABEQ
instname_str Associação Brasileira de Engenharia Química (ABEQ)
instacron_str ABEQ
institution ABEQ
reponame_str Brazilian Journal of Chemical Engineering
collection Brazilian Journal of Chemical Engineering
repository.name.fl_str_mv Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)
repository.mail.fl_str_mv rgiudici@usp.br||rgiudici@usp.br
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