Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09
Main Author: | |
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Publication Date: | 2016 |
Other Authors: | , , |
Format: | Article |
Language: | eng |
Source: | Anais da Academia Brasileira de Ciências (Online) |
Download full: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000200479 |
Summary: | ABSTRACT A soil isolate, Penicillium janthinellum sw09 has been found to produce significant amounts of an extracellular pectinase subsequently characterized as exo-polygalacturonase (exo-PG). By optimizing growth conditions, P. janthinellum sw09 produced high amount of exo-PG (16.54 units/mL). The crude enzyme was purified by gel filtration chromatography and two exo-PG activity peaks (designated as PGI and PGII) were revealed. On SDS-PAGE analysis, purified PGII using DEAE-Sepharose FF column, was found to be a single band with a molecular mass of 66.2 kDa. The purified PGII exhibited maximal activity at the temperature of 45 oC and pH 5.0. The stability profiles show that PGII is more stable in the pH range of 4.0-8.0 and below 60 oC. The Km and Vmax for the enzyme was 1.74 mg/mL and 18.08 μmol/ (mL•min), respectively. Due to this enzymatic characterization, this pectinase is an attractive candidate for applications in degradation of pectin. |
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Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09Penicillium janthinellumpolygalacturonasepurificationcharacterizationABSTRACT A soil isolate, Penicillium janthinellum sw09 has been found to produce significant amounts of an extracellular pectinase subsequently characterized as exo-polygalacturonase (exo-PG). By optimizing growth conditions, P. janthinellum sw09 produced high amount of exo-PG (16.54 units/mL). The crude enzyme was purified by gel filtration chromatography and two exo-PG activity peaks (designated as PGI and PGII) were revealed. On SDS-PAGE analysis, purified PGII using DEAE-Sepharose FF column, was found to be a single band with a molecular mass of 66.2 kDa. The purified PGII exhibited maximal activity at the temperature of 45 oC and pH 5.0. The stability profiles show that PGII is more stable in the pH range of 4.0-8.0 and below 60 oC. The Km and Vmax for the enzyme was 1.74 mg/mL and 18.08 μmol/ (mL•min), respectively. Due to this enzymatic characterization, this pectinase is an attractive candidate for applications in degradation of pectin.Academia Brasileira de Ciências2016-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000200479Anais da Academia Brasileira de Ciências v.88 suppl.1 2016reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765201620150051info:eu-repo/semantics/openAccessMA,YUPINGSUN,SIWENHAO,HUIXU,CHUNPINGeng2016-06-17T00:00:00Zoai:scielo:S0001-37652016000200479Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2016-06-17T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false |
dc.title.none.fl_str_mv |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
title |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
spellingShingle |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 MA,YUPING Penicillium janthinellum polygalacturonase purification characterization |
title_short |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
title_full |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
title_fullStr |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
title_full_unstemmed |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
title_sort |
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 |
author |
MA,YUPING |
author_facet |
MA,YUPING SUN,SIWEN HAO,HUI XU,CHUNPING |
author_role |
author |
author2 |
SUN,SIWEN HAO,HUI XU,CHUNPING |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
MA,YUPING SUN,SIWEN HAO,HUI XU,CHUNPING |
dc.subject.por.fl_str_mv |
Penicillium janthinellum polygalacturonase purification characterization |
topic |
Penicillium janthinellum polygalacturonase purification characterization |
description |
ABSTRACT A soil isolate, Penicillium janthinellum sw09 has been found to produce significant amounts of an extracellular pectinase subsequently characterized as exo-polygalacturonase (exo-PG). By optimizing growth conditions, P. janthinellum sw09 produced high amount of exo-PG (16.54 units/mL). The crude enzyme was purified by gel filtration chromatography and two exo-PG activity peaks (designated as PGI and PGII) were revealed. On SDS-PAGE analysis, purified PGII using DEAE-Sepharose FF column, was found to be a single band with a molecular mass of 66.2 kDa. The purified PGII exhibited maximal activity at the temperature of 45 oC and pH 5.0. The stability profiles show that PGII is more stable in the pH range of 4.0-8.0 and below 60 oC. The Km and Vmax for the enzyme was 1.74 mg/mL and 18.08 μmol/ (mL•min), respectively. Due to this enzymatic characterization, this pectinase is an attractive candidate for applications in degradation of pectin. |
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=S0001-37652016000200479 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000200479 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/0001-3765201620150051 |
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 |
Academia Brasileira de Ciências |
publisher.none.fl_str_mv |
Academia Brasileira de Ciências |
dc.source.none.fl_str_mv |
Anais da Academia Brasileira de Ciências v.88 suppl.1 2016 reponame:Anais da Academia Brasileira de Ciências (Online) instname:Academia Brasileira de Ciências (ABC) instacron:ABC |
instname_str |
Academia Brasileira de Ciências (ABC) |
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ABC |
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ABC |
reponame_str |
Anais da Academia Brasileira de Ciências (Online) |
collection |
Anais da Academia Brasileira de Ciências (Online) |
repository.name.fl_str_mv |
Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC) |
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||aabc@abc.org.br |
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1754302862784987136 |