Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci
Autor(a) principal: | |
---|---|
Data de Publicação: | 2016 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000300741 |
Resumo: | ABSTRACT Aminotransferases and glutamate dehydrogenase are two main types of enzymes involved in the initial steps of amino acid catabolism, which plays a key role in the cheese flavor development. In the present work, glutamate dehydrogenase and aminotransferase activities were screened in twenty one strains of lactic acid bacteria of dairy interest, either cheese-isolated or commercial starters, including fifteen mesophilic lactobacilli, four thermophilic lactobacilli, and two streptococci. The strains of Streptococcus thermophilus showed the highest glutamate dehydrogenase activity, which was significantly elevated compared with the lactobacilli. Aspartate aminotransferase prevailed in most strains tested, while the levels and specificity of other aminotransferases were highly strain- and species-dependent. The knowledge of enzymatic profiles of these starter and cheese-isolated cultures is helpful in proposing appropriate combinations of strains for improved or increased cheese flavor. |
id |
SBM-1_44efe34de7ab118fd0ecd551e8555787 |
---|---|
oai_identifier_str |
oai:scielo:S1517-83822016000300741 |
network_acronym_str |
SBM-1 |
network_name_str |
Brazilian Journal of Microbiology |
repository_id_str |
|
spelling |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococciAminotransferase activityGlutamate dehydrogenase activityLactobacilliStreptococciABSTRACT Aminotransferases and glutamate dehydrogenase are two main types of enzymes involved in the initial steps of amino acid catabolism, which plays a key role in the cheese flavor development. In the present work, glutamate dehydrogenase and aminotransferase activities were screened in twenty one strains of lactic acid bacteria of dairy interest, either cheese-isolated or commercial starters, including fifteen mesophilic lactobacilli, four thermophilic lactobacilli, and two streptococci. The strains of Streptococcus thermophilus showed the highest glutamate dehydrogenase activity, which was significantly elevated compared with the lactobacilli. Aspartate aminotransferase prevailed in most strains tested, while the levels and specificity of other aminotransferases were highly strain- and species-dependent. The knowledge of enzymatic profiles of these starter and cheese-isolated cultures is helpful in proposing appropriate combinations of strains for improved or increased cheese flavor.Sociedade Brasileira de Microbiologia2016-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000300741Brazilian Journal of Microbiology v.47 n.3 2016reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1016/j.bjm.2016.04.005info:eu-repo/semantics/openAccessPeralta,Guillermo HugoBergamini,Carina VivianaHynes,Erica Ruteng2016-08-02T00:00:00Zoai:scielo:S1517-83822016000300741Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2016-08-02T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
title |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
spellingShingle |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci Peralta,Guillermo Hugo Aminotransferase activity Glutamate dehydrogenase activity Lactobacilli Streptococci |
title_short |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
title_full |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
title_fullStr |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
title_full_unstemmed |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
title_sort |
Aminotransferase and glutamate dehydrogenase activities in lactobacilli and streptococci |
author |
Peralta,Guillermo Hugo |
author_facet |
Peralta,Guillermo Hugo Bergamini,Carina Viviana Hynes,Erica Rut |
author_role |
author |
author2 |
Bergamini,Carina Viviana Hynes,Erica Rut |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Peralta,Guillermo Hugo Bergamini,Carina Viviana Hynes,Erica Rut |
dc.subject.por.fl_str_mv |
Aminotransferase activity Glutamate dehydrogenase activity Lactobacilli Streptococci |
topic |
Aminotransferase activity Glutamate dehydrogenase activity Lactobacilli Streptococci |
description |
ABSTRACT Aminotransferases and glutamate dehydrogenase are two main types of enzymes involved in the initial steps of amino acid catabolism, which plays a key role in the cheese flavor development. In the present work, glutamate dehydrogenase and aminotransferase activities were screened in twenty one strains of lactic acid bacteria of dairy interest, either cheese-isolated or commercial starters, including fifteen mesophilic lactobacilli, four thermophilic lactobacilli, and two streptococci. The strains of Streptococcus thermophilus showed the highest glutamate dehydrogenase activity, which was significantly elevated compared with the lactobacilli. Aspartate aminotransferase prevailed in most strains tested, while the levels and specificity of other aminotransferases were highly strain- and species-dependent. The knowledge of enzymatic profiles of these starter and cheese-isolated cultures is helpful in proposing appropriate combinations of strains for improved or increased cheese flavor. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-09-01 |
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=S1517-83822016000300741 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000300741 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1016/j.bjm.2016.04.005 |
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 Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.47 n.3 2016 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122208461783040 |