Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk

Detalhes bibliográficos
Autor(a) principal: BOSSO,Alessandra
Data de Publicação: 2016
Outros Autores: MORIOKA,Luiz Rodrigo Ito, SANTOS,Leandro Freire dos, SUGUIMOTO,Hélio Hiroshi
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Food Science and Technology (Campinas)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612016000100159
Resumo: Abstract The commercial enzyme (E.C. = 3.2.1.23) from Kluyveromyces lactis (liquid) and Aspergillus oryzae(lyophilized) was investigated for its hydrolysis potential in lactose substrate, UHT milk, and skimmed milk at different concentrations (0.7; 1.0 and 1.5%), pH values (5.0; 6.0; 6.5 and 7.0), and temperature (30; 35; 40 and 55 ºC). High hydrolysis rates were observed for the enzyme from K. lactis at pH 7.0 and 40 ºC, and from A. oryzae at pH 5.0 and 55 ºC. The enzyme from K. lactis showed significantly higher hydrolysis rates when compared to A. oryzae. The effect of temperature and β-galactosidase concentration on the lactose hydrolysis in UHT milk was higher than in skimmed milk, for all temperatures tested. With respect to the thermal stability, a decrease in hydrolysis rate was observed at pH 6.0 at 35 ºC for K. lactisenzyme, and at pH 6.0 at 55 ºC for the enzyme from A. oryzae. This study investigate the hydrolysis of β-galactosidase in UHT and skimmed milk. The knowledge about the characteristics of the β-galactosidase fromK. lactis and A. oryzae enables to use it most efficiently to control the enzyme concentration, temperature, and pH in many industrial processes and product formulations.
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spelling Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milkUHT and skimmed milkβ-galactosidaseenzymatic characterizationlactose intoleranceenzyme activityAbstract The commercial enzyme (E.C. = 3.2.1.23) from Kluyveromyces lactis (liquid) and Aspergillus oryzae(lyophilized) was investigated for its hydrolysis potential in lactose substrate, UHT milk, and skimmed milk at different concentrations (0.7; 1.0 and 1.5%), pH values (5.0; 6.0; 6.5 and 7.0), and temperature (30; 35; 40 and 55 ºC). High hydrolysis rates were observed for the enzyme from K. lactis at pH 7.0 and 40 ºC, and from A. oryzae at pH 5.0 and 55 ºC. The enzyme from K. lactis showed significantly higher hydrolysis rates when compared to A. oryzae. The effect of temperature and β-galactosidase concentration on the lactose hydrolysis in UHT milk was higher than in skimmed milk, for all temperatures tested. With respect to the thermal stability, a decrease in hydrolysis rate was observed at pH 6.0 at 35 ºC for K. lactisenzyme, and at pH 6.0 at 55 ºC for the enzyme from A. oryzae. This study investigate the hydrolysis of β-galactosidase in UHT and skimmed milk. The knowledge about the characteristics of the β-galactosidase fromK. lactis and A. oryzae enables to use it most efficiently to control the enzyme concentration, temperature, and pH in many industrial processes and product formulations.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2016-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612016000100159Food Science and Technology v.36 n.1 2016reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/1678-457X.0085info:eu-repo/semantics/openAccessBOSSO,AlessandraMORIOKA,Luiz Rodrigo ItoSANTOS,Leandro Freire dosSUGUIMOTO,Hélio Hiroshieng2016-04-12T00:00:00Zoai:scielo:S0101-20612016000100159Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2016-04-12T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false
dc.title.none.fl_str_mv Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
title Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
spellingShingle Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
BOSSO,Alessandra
UHT and skimmed milk
β-galactosidase
enzymatic characterization
lactose intolerance
enzyme activity
title_short Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
title_full Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
title_fullStr Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
title_full_unstemmed Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
title_sort Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
author BOSSO,Alessandra
author_facet BOSSO,Alessandra
MORIOKA,Luiz Rodrigo Ito
SANTOS,Leandro Freire dos
SUGUIMOTO,Hélio Hiroshi
author_role author
author2 MORIOKA,Luiz Rodrigo Ito
SANTOS,Leandro Freire dos
SUGUIMOTO,Hélio Hiroshi
author2_role author
author
author
dc.contributor.author.fl_str_mv BOSSO,Alessandra
MORIOKA,Luiz Rodrigo Ito
SANTOS,Leandro Freire dos
SUGUIMOTO,Hélio Hiroshi
dc.subject.por.fl_str_mv UHT and skimmed milk
β-galactosidase
enzymatic characterization
lactose intolerance
enzyme activity
topic UHT and skimmed milk
β-galactosidase
enzymatic characterization
lactose intolerance
enzyme activity
description Abstract The commercial enzyme (E.C. = 3.2.1.23) from Kluyveromyces lactis (liquid) and Aspergillus oryzae(lyophilized) was investigated for its hydrolysis potential in lactose substrate, UHT milk, and skimmed milk at different concentrations (0.7; 1.0 and 1.5%), pH values (5.0; 6.0; 6.5 and 7.0), and temperature (30; 35; 40 and 55 ºC). High hydrolysis rates were observed for the enzyme from K. lactis at pH 7.0 and 40 ºC, and from A. oryzae at pH 5.0 and 55 ºC. The enzyme from K. lactis showed significantly higher hydrolysis rates when compared to A. oryzae. The effect of temperature and β-galactosidase concentration on the lactose hydrolysis in UHT milk was higher than in skimmed milk, for all temperatures tested. With respect to the thermal stability, a decrease in hydrolysis rate was observed at pH 6.0 at 35 ºC for K. lactisenzyme, and at pH 6.0 at 55 ºC for the enzyme from A. oryzae. This study investigate the hydrolysis of β-galactosidase in UHT and skimmed milk. The knowledge about the characteristics of the β-galactosidase fromK. lactis and A. oryzae enables to use it most efficiently to control the enzyme concentration, temperature, and pH in many industrial processes and product formulations.
publishDate 2016
dc.date.none.fl_str_mv 2016-03-01
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=S0101-20612016000100159
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612016000100159
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-457X.0085
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 Sociedade Brasileira de Ciência e Tecnologia de Alimentos
publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
dc.source.none.fl_str_mv Food Science and Technology v.36 n.1 2016
reponame:Food Science and Technology (Campinas)
instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron:SBCTA
instname_str Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron_str SBCTA
institution SBCTA
reponame_str Food Science and Technology (Campinas)
collection Food Science and Technology (Campinas)
repository.name.fl_str_mv Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
repository.mail.fl_str_mv ||revista@sbcta.org.br
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