Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Ciência Rural |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782016000500921 |
Resumo: | ABSTRACT: One of the greatest challenges for dairy industries is the correct destination of all the whey generated during cheese making, considering its high impact, the large volume created, and its technological potential. Enzymatic hydrolysis of cheese whey lactose is a biotechnological alternative. However, one of the limiting factors of its use is the relatively high cost of the enzymes, which could be lowered with the immobilization of these biocatalysts. Considering this context, the objective of this research was to evaluate the commercial Kluyveromyces lactis β-galactosidase enzyme immobilized in calcium alginate spheres and gelatin, using glutaraldehyde and concanavalin A (ConA) as modifying agents in the hydrolysis of cheese whey lactose process. Results have shown that the enzyme encapsulation complexed with ConA in alginate-gelatin spheres, without glutaraldehyde in the immobilization support, has significantly increased the hydrolysis of lactose rate, achieving a maximum conversion of 72%. |
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Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactoselactosecheese wheyβ-galactosidaseenzyme immobilizationABSTRACT: One of the greatest challenges for dairy industries is the correct destination of all the whey generated during cheese making, considering its high impact, the large volume created, and its technological potential. Enzymatic hydrolysis of cheese whey lactose is a biotechnological alternative. However, one of the limiting factors of its use is the relatively high cost of the enzymes, which could be lowered with the immobilization of these biocatalysts. Considering this context, the objective of this research was to evaluate the commercial Kluyveromyces lactis β-galactosidase enzyme immobilized in calcium alginate spheres and gelatin, using glutaraldehyde and concanavalin A (ConA) as modifying agents in the hydrolysis of cheese whey lactose process. Results have shown that the enzyme encapsulation complexed with ConA in alginate-gelatin spheres, without glutaraldehyde in the immobilization support, has significantly increased the hydrolysis of lactose rate, achieving a maximum conversion of 72%.Universidade Federal de Santa Maria2016-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782016000500921Ciência Rural v.46 n.5 2016reponame:Ciência Ruralinstname:Universidade Federal de Santa Maria (UFSM)instacron:UFSM10.1590/0103-8478cr20150833info:eu-repo/semantics/openAccessMörschbächer,Ana PaulaVolpato,GiandraSouza,Claucia Fernanda Volken deeng2016-10-20T00:00:00ZRevista |
dc.title.none.fl_str_mv |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
title |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
spellingShingle |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose Mörschbächer,Ana Paula lactose cheese whey β-galactosidase enzyme immobilization |
title_short |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
title_full |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
title_fullStr |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
title_full_unstemmed |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
title_sort |
Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose |
author |
Mörschbächer,Ana Paula |
author_facet |
Mörschbächer,Ana Paula Volpato,Giandra Souza,Claucia Fernanda Volken de |
author_role |
author |
author2 |
Volpato,Giandra Souza,Claucia Fernanda Volken de |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Mörschbächer,Ana Paula Volpato,Giandra Souza,Claucia Fernanda Volken de |
dc.subject.por.fl_str_mv |
lactose cheese whey β-galactosidase enzyme immobilization |
topic |
lactose cheese whey β-galactosidase enzyme immobilization |
description |
ABSTRACT: One of the greatest challenges for dairy industries is the correct destination of all the whey generated during cheese making, considering its high impact, the large volume created, and its technological potential. Enzymatic hydrolysis of cheese whey lactose is a biotechnological alternative. However, one of the limiting factors of its use is the relatively high cost of the enzymes, which could be lowered with the immobilization of these biocatalysts. Considering this context, the objective of this research was to evaluate the commercial Kluyveromyces lactis β-galactosidase enzyme immobilized in calcium alginate spheres and gelatin, using glutaraldehyde and concanavalin A (ConA) as modifying agents in the hydrolysis of cheese whey lactose process. Results have shown that the enzyme encapsulation complexed with ConA in alginate-gelatin spheres, without glutaraldehyde in the immobilization support, has significantly increased the hydrolysis of lactose rate, achieving a maximum conversion of 72%. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-05-01 |
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=S0103-84782016000500921 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782016000500921 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/0103-8478cr20150833 |
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 |
Universidade Federal de Santa Maria |
publisher.none.fl_str_mv |
Universidade Federal de Santa Maria |
dc.source.none.fl_str_mv |
Ciência Rural v.46 n.5 2016 reponame:Ciência Rural instname:Universidade Federal de Santa Maria (UFSM) instacron:UFSM |
instname_str |
Universidade Federal de Santa Maria (UFSM) |
instacron_str |
UFSM |
institution |
UFSM |
reponame_str |
Ciência Rural |
collection |
Ciência Rural |
repository.name.fl_str_mv |
|
repository.mail.fl_str_mv |
|
_version_ |
1749140549063933952 |