Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , |
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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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 |
_version_ |
1752126320448372736 |