Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Detalhes bibliográficos
Autor(a) principal: Baltas,Nimet
Data de Publicação: 2016
Outros Autores: Dincer,Barbaros, Ekinci,Arife Pinar, Kolayli,Sevgi, Adiguzel,Ahmet
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=S1516-89132016000100605
Resumo: ABSTRACT α-Amylase from Anoxybacillus thermarum A4 was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration chromatography, with 29.8-fold purification and 74.6% yield. A4 amylase showed best performance for soluble potato starch hydrolysis at 70 °C and pH 5.5-10.5. A4 amylase was extremely stable at +4 °C, and the enzyme retained over 65% of its original α-amylase activity at 70 °C and 43% at 90 °C. The enzyme's Km values for soluble starch, amylopectin and amylose substrates were obtained as 0.9, 1.3 and 0.5 mg/mL, respectively. EDTA, Hg2+, B4O7 2-, OH-, CN- , and urea exhibited different inhibition effects; their IC50 values were identified as 8.0, 5.75, 16.5, 15.2, 8.2 and 10.9 mM, respectively. A4 amylase exhibited extreme stability toward some surfactants and perfect match for a wide variety of commercial solid and liquid detergents at 55 °C. So, it may be considered to be potential applications for detergent and other industrial uses.
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spelling Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strainAnoxybacillus thermarum A4Extracellular α-AmylaseHighly thermostablePurificationABSTRACT α-Amylase from Anoxybacillus thermarum A4 was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration chromatography, with 29.8-fold purification and 74.6% yield. A4 amylase showed best performance for soluble potato starch hydrolysis at 70 °C and pH 5.5-10.5. A4 amylase was extremely stable at +4 °C, and the enzyme retained over 65% of its original α-amylase activity at 70 °C and 43% at 90 °C. The enzyme's Km values for soluble starch, amylopectin and amylose substrates were obtained as 0.9, 1.3 and 0.5 mg/mL, respectively. EDTA, Hg2+, B4O7 2-, OH-, CN- , and urea exhibited different inhibition effects; their IC50 values were identified as 8.0, 5.75, 16.5, 15.2, 8.2 and 10.9 mM, respectively. A4 amylase exhibited extreme stability toward some surfactants and perfect match for a wide variety of commercial solid and liquid detergents at 55 °C. So, it may be considered to be potential applications for detergent and other industrial uses.Instituto de Tecnologia do Paraná - Tecpar2016-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132016000100605Brazilian Archives of Biology and Technology v.59 2016reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/1678-4324-2016160346info:eu-repo/semantics/openAccessBaltas,NimetDincer,BarbarosEkinci,Arife PinarKolayli,SevgiAdiguzel,Ahmeteng2018-06-27T00:00:00Zoai:scielo:S1516-89132016000100605Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2018-06-27T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
title Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
spellingShingle Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
Baltas,Nimet
Anoxybacillus thermarum A4
Extracellular α-Amylase
Highly thermostable
Purification
title_short Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
title_full Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
title_fullStr Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
title_full_unstemmed Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
title_sort Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
author Baltas,Nimet
author_facet Baltas,Nimet
Dincer,Barbaros
Ekinci,Arife Pinar
Kolayli,Sevgi
Adiguzel,Ahmet
author_role author
author2 Dincer,Barbaros
Ekinci,Arife Pinar
Kolayli,Sevgi
Adiguzel,Ahmet
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Baltas,Nimet
Dincer,Barbaros
Ekinci,Arife Pinar
Kolayli,Sevgi
Adiguzel,Ahmet
dc.subject.por.fl_str_mv Anoxybacillus thermarum A4
Extracellular α-Amylase
Highly thermostable
Purification
topic Anoxybacillus thermarum A4
Extracellular α-Amylase
Highly thermostable
Purification
description ABSTRACT α-Amylase from Anoxybacillus thermarum A4 was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration chromatography, with 29.8-fold purification and 74.6% yield. A4 amylase showed best performance for soluble potato starch hydrolysis at 70 °C and pH 5.5-10.5. A4 amylase was extremely stable at +4 °C, and the enzyme retained over 65% of its original α-amylase activity at 70 °C and 43% at 90 °C. The enzyme's Km values for soluble starch, amylopectin and amylose substrates were obtained as 0.9, 1.3 and 0.5 mg/mL, respectively. EDTA, Hg2+, B4O7 2-, OH-, CN- , and urea exhibited different inhibition effects; their IC50 values were identified as 8.0, 5.75, 16.5, 15.2, 8.2 and 10.9 mM, respectively. A4 amylase exhibited extreme stability toward some surfactants and perfect match for a wide variety of commercial solid and liquid detergents at 55 °C. So, it may be considered to be potential applications for detergent and other industrial uses.
publishDate 2016
dc.date.none.fl_str_mv 2016-01-01
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=S1516-89132016000100605
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132016000100605
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-4324-2016160346
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.59 2016
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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