Control of Acid Phosphatases Expression from Aspergillus niger by Soil Characteristics
Autor(a) principal: | |
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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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Brazilian Archives of Biology and Technology |
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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 |
_version_ |
1750318276952457216 |