Bacterial phytase: potential application, in vivo function and regulation of its synthesis
Autor(a) principal: | |
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Data de Publicação: | 2004 |
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=S1517-83822004000100002 |
Resumo: | The stepwise release of phosphate from phytate, the major storage form of phosphate in plant seeds and pollen, is initiated by a class of enzymes that have been collectively called phytases. The classification is solely due to the in vitro capability of these enzymes to accept phytate as a substrate. Phytases have been studied intensively in recent years because of the great interest in such enzymes for reducing phytate content in animal feed and food for human consumption. They have a wide distribution in plants, microorganisms, and in some animal tissues. Due to several biological characteristics, such as substrate specificity, resistance to proteolysis and catalytic efficiency, bacterial phytases have considerable potential in commercial applications. In bacteria, phytase is an inducible enzyme and its expression is subjected to a complex regulation, but phytase formation is not controlled uniformly among different bacteria. It was suggested that phytase is not required for balanced growth of bacterial cells, but may be synthesised in response to a nutrient or energy limitation. |
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Brazilian Journal of Microbiology |
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Bacterial phytase: potential application, in vivo function and regulation of its synthesisbacterial phytasebiotechnological applicationdephosphorylationoccurrencephytase formationphytateThe stepwise release of phosphate from phytate, the major storage form of phosphate in plant seeds and pollen, is initiated by a class of enzymes that have been collectively called phytases. The classification is solely due to the in vitro capability of these enzymes to accept phytate as a substrate. Phytases have been studied intensively in recent years because of the great interest in such enzymes for reducing phytate content in animal feed and food for human consumption. They have a wide distribution in plants, microorganisms, and in some animal tissues. Due to several biological characteristics, such as substrate specificity, resistance to proteolysis and catalytic efficiency, bacterial phytases have considerable potential in commercial applications. In bacteria, phytase is an inducible enzyme and its expression is subjected to a complex regulation, but phytase formation is not controlled uniformly among different bacteria. It was suggested that phytase is not required for balanced growth of bacterial cells, but may be synthesised in response to a nutrient or energy limitation.Sociedade Brasileira de Microbiologia2004-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100002Brazilian Journal of Microbiology v.35 n.1-2 2004reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822004000100002info:eu-repo/semantics/openAccessKonietzny,UrsulaGreiner,Ralfeng2004-11-16T00:00:00Zoai:scielo:S1517-83822004000100002Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2004-11-16T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
title |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
spellingShingle |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis Konietzny,Ursula bacterial phytase biotechnological application dephosphorylation occurrence phytase formation phytate |
title_short |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
title_full |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
title_fullStr |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
title_full_unstemmed |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
title_sort |
Bacterial phytase: potential application, in vivo function and regulation of its synthesis |
author |
Konietzny,Ursula |
author_facet |
Konietzny,Ursula Greiner,Ralf |
author_role |
author |
author2 |
Greiner,Ralf |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Konietzny,Ursula Greiner,Ralf |
dc.subject.por.fl_str_mv |
bacterial phytase biotechnological application dephosphorylation occurrence phytase formation phytate |
topic |
bacterial phytase biotechnological application dephosphorylation occurrence phytase formation phytate |
description |
The stepwise release of phosphate from phytate, the major storage form of phosphate in plant seeds and pollen, is initiated by a class of enzymes that have been collectively called phytases. The classification is solely due to the in vitro capability of these enzymes to accept phytate as a substrate. Phytases have been studied intensively in recent years because of the great interest in such enzymes for reducing phytate content in animal feed and food for human consumption. They have a wide distribution in plants, microorganisms, and in some animal tissues. Due to several biological characteristics, such as substrate specificity, resistance to proteolysis and catalytic efficiency, bacterial phytases have considerable potential in commercial applications. In bacteria, phytase is an inducible enzyme and its expression is subjected to a complex regulation, but phytase formation is not controlled uniformly among different bacteria. It was suggested that phytase is not required for balanced growth of bacterial cells, but may be synthesised in response to a nutrient or energy limitation. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-06-01 |
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=S1517-83822004000100002 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100002 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822004000100002 |
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.35 n.1-2 2004 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_ |
1752122199800545280 |