Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis

Detalhes bibliográficos
Autor(a) principal: Satar,Rukhsana
Data de Publicação: 2017
Outros Autores: Ansari,Shakeel Ahmed
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=S0104-66322017000200451
Resumo: Abstract The present study demonstrates the immobilization of β-galactosidase from Cicer arietinum on a simple and inexpensive matrix, glutaraldehyde functionalized agarose (GFA), to suggest its potential application in hydrolyzing whey lactose in biotechnology industries. The designed matrix provided large surface area for the immobilization of β-galactosidase, apart from exhibiting greater biocatalytic activity in terms of selectivity, loading and stability. GFA retained 83% enzyme activity as a result of immobilization. Soluble and GFA bound Cicer arietinum β-galactosidase showed the same pH and temperature-optima at pH 5.0 and at 50 °C, respectively. However, immobilized enzyme exhibited a greater fraction of activity at both acidic and basic pH, and at higher temperature ranges. GFA bound enzyme lost only 20 % enzyme in the presence of 3% galactose, and retained 70 % activity even after its sixth repeated use. Immobilized enzyme showed pronounced lactose hydrolysis from whey in batch processes at 55 °C as compared to enzyme in solution.
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spelling Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysisagaroseβ-galactosidaseCicer arietinumglutaraldehydewhey hydrolysisAbstract The present study demonstrates the immobilization of β-galactosidase from Cicer arietinum on a simple and inexpensive matrix, glutaraldehyde functionalized agarose (GFA), to suggest its potential application in hydrolyzing whey lactose in biotechnology industries. The designed matrix provided large surface area for the immobilization of β-galactosidase, apart from exhibiting greater biocatalytic activity in terms of selectivity, loading and stability. GFA retained 83% enzyme activity as a result of immobilization. Soluble and GFA bound Cicer arietinum β-galactosidase showed the same pH and temperature-optima at pH 5.0 and at 50 °C, respectively. However, immobilized enzyme exhibited a greater fraction of activity at both acidic and basic pH, and at higher temperature ranges. GFA bound enzyme lost only 20 % enzyme in the presence of 3% galactose, and retained 70 % activity even after its sixth repeated use. Immobilized enzyme showed pronounced lactose hydrolysis from whey in batch processes at 55 °C as compared to enzyme in solution.Brazilian Society of Chemical Engineering2017-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322017000200451Brazilian Journal of Chemical Engineering v.34 n.2 2017reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/0104-6632.20170342s20160107info:eu-repo/semantics/openAccessSatar,RukhsanaAnsari,Shakeel Ahmedeng2017-10-05T00:00:00Zoai:scielo:S0104-66322017000200451Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2017-10-05T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
title Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
spellingShingle Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
Satar,Rukhsana
agarose
β-galactosidase
Cicer arietinum
glutaraldehyde
whey hydrolysis
title_short Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
title_full Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
title_fullStr Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
title_full_unstemmed Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
title_sort Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis
author Satar,Rukhsana
author_facet Satar,Rukhsana
Ansari,Shakeel Ahmed
author_role author
author2 Ansari,Shakeel Ahmed
author2_role author
dc.contributor.author.fl_str_mv Satar,Rukhsana
Ansari,Shakeel Ahmed
dc.subject.por.fl_str_mv agarose
β-galactosidase
Cicer arietinum
glutaraldehyde
whey hydrolysis
topic agarose
β-galactosidase
Cicer arietinum
glutaraldehyde
whey hydrolysis
description Abstract The present study demonstrates the immobilization of β-galactosidase from Cicer arietinum on a simple and inexpensive matrix, glutaraldehyde functionalized agarose (GFA), to suggest its potential application in hydrolyzing whey lactose in biotechnology industries. The designed matrix provided large surface area for the immobilization of β-galactosidase, apart from exhibiting greater biocatalytic activity in terms of selectivity, loading and stability. GFA retained 83% enzyme activity as a result of immobilization. Soluble and GFA bound Cicer arietinum β-galactosidase showed the same pH and temperature-optima at pH 5.0 and at 50 °C, respectively. However, immobilized enzyme exhibited a greater fraction of activity at both acidic and basic pH, and at higher temperature ranges. GFA bound enzyme lost only 20 % enzyme in the presence of 3% galactose, and retained 70 % activity even after its sixth repeated use. Immobilized enzyme showed pronounced lactose hydrolysis from whey in batch processes at 55 °C as compared to enzyme in solution.
publishDate 2017
dc.date.none.fl_str_mv 2017-04-01
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=S0104-66322017000200451
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322017000200451
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0104-6632.20170342s20160107
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.34 n.2 2017
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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