Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics

Detalhes bibliográficos
Autor(a) principal: Nahas,Ely
Data de Publicação: 2015
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000500658
Resumo: ABSTRACTThis work studied the acid phosphatase (APase) activity from culture medium (extracellular, eAPase) and mycelial extract (intracellular, iAPase) ofAspergillus niger F111. The influence of fungus growth and phosphate concentration of the media on the synthesis and secretion of phosphatase was demonstrated. The effects of pH, substrate concentration and inorganic and organic compounds added to the reaction mixture on APase activity were also studied. Both enzymes were repressed by high concentrations of phosphate. Overexpression of iAPase in relation to eAPase was detected; iAPase activity was 46.1 times higher than eAPase. The maximal activity of eAPase was after 24h of fungus growth and for iAPase was after 96h. Optimal pH and substrate concentrations were 4.5 and 8.0 mM, respectively. Michaelis-Menten constant (Km) for the hydrolysis of p-nitrophenyl phosphate was 0.57 mM with Vmax = 14,285.71 U mg-1 mycelium for the iAPase and 0.31 mM with V max = 147.06 U mg-1 mycelium for eAPase. Organic substances had little effect on acid phosphatases when compared with the salts. Both the APases were inhibited by 10 mM KH 2PO4 and 5 mM (NH4)2MoO4; eAPase was also inhibited by 1 mM CoCl2.
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spelling Control of Acid Phosphatases Expression from Aspergillus niger by Soil CharacteristicsEnzyme inhibitorsmolybdenumoverexpressionphosphatesoil chemical characteristicsABSTRACTThis work studied the acid phosphatase (APase) activity from culture medium (extracellular, eAPase) and mycelial extract (intracellular, iAPase) ofAspergillus niger F111. The influence of fungus growth and phosphate concentration of the media on the synthesis and secretion of phosphatase was demonstrated. The effects of pH, substrate concentration and inorganic and organic compounds added to the reaction mixture on APase activity were also studied. Both enzymes were repressed by high concentrations of phosphate. Overexpression of iAPase in relation to eAPase was detected; iAPase activity was 46.1 times higher than eAPase. The maximal activity of eAPase was after 24h of fungus growth and for iAPase was after 96h. Optimal pH and substrate concentrations were 4.5 and 8.0 mM, respectively. Michaelis-Menten constant (Km) for the hydrolysis of p-nitrophenyl phosphate was 0.57 mM with Vmax = 14,285.71 U mg-1 mycelium for the iAPase and 0.31 mM with V max = 147.06 U mg-1 mycelium for eAPase. Organic substances had little effect on acid phosphatases when compared with the salts. Both the APases were inhibited by 10 mM KH 2PO4 and 5 mM (NH4)2MoO4; eAPase was also inhibited by 1 mM CoCl2.Instituto de Tecnologia do Paraná - Tecpar2015-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000500658Brazilian Archives of Biology and Technology v.58 n.5 2015reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132015050485info:eu-repo/semantics/openAccessNahas,Elyeng2015-11-06T00:00:00Zoai:scielo:S1516-89132015000500658Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-11-06T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
title Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
spellingShingle Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
Nahas,Ely
Enzyme inhibitors
molybdenum
overexpression
phosphate
soil chemical characteristics
title_short Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
title_full Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
title_fullStr Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
title_full_unstemmed Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
title_sort Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
author Nahas,Ely
author_facet Nahas,Ely
author_role author
dc.contributor.author.fl_str_mv Nahas,Ely
dc.subject.por.fl_str_mv Enzyme inhibitors
molybdenum
overexpression
phosphate
soil chemical characteristics
topic Enzyme inhibitors
molybdenum
overexpression
phosphate
soil chemical characteristics
description ABSTRACTThis work studied the acid phosphatase (APase) activity from culture medium (extracellular, eAPase) and mycelial extract (intracellular, iAPase) ofAspergillus niger F111. The influence of fungus growth and phosphate concentration of the media on the synthesis and secretion of phosphatase was demonstrated. The effects of pH, substrate concentration and inorganic and organic compounds added to the reaction mixture on APase activity were also studied. Both enzymes were repressed by high concentrations of phosphate. Overexpression of iAPase in relation to eAPase was detected; iAPase activity was 46.1 times higher than eAPase. The maximal activity of eAPase was after 24h of fungus growth and for iAPase was after 96h. Optimal pH and substrate concentrations were 4.5 and 8.0 mM, respectively. Michaelis-Menten constant (Km) for the hydrolysis of p-nitrophenyl phosphate was 0.57 mM with Vmax = 14,285.71 U mg-1 mycelium for the iAPase and 0.31 mM with V max = 147.06 U mg-1 mycelium for eAPase. Organic substances had little effect on acid phosphatases when compared with the salts. Both the APases were inhibited by 10 mM KH 2PO4 and 5 mM (NH4)2MoO4; eAPase was also inhibited by 1 mM CoCl2.
publishDate 2015
dc.date.none.fl_str_mv 2015-10-01
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=S1516-89132015000500658
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000500658
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-89132015050485
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 Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.58 n.5 2015
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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