Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09

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...

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Main Authors: YUPING MA, SIWEN SUN, HUI HAO, CHUNPING XU
Format: Article
Language:English
Published: Academia Brasileira de Ciências 2016-01-01
Series:Anais da Academia Brasileira de Ciências
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000200479&lng=en&tlng=en
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spelling doaj-e6c304bd8f324b658217f01be72694ea2020-11-25T00:21:01ZengAcademia Brasileira de CiênciasAnais da Academia Brasileira de Ciências1678-26902016-01-0188suppl 147948710.1590/0001-3765201620150051S0001-37652016000200479Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09YUPING MASIWEN SUNHUI HAOCHUNPING XUABSTRACT 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000200479&lng=en&tlng=enPenicillium janthinellumpoligalacturonasepurificaçãocaracterização
collection DOAJ
language English
format Article
sources DOAJ
author YUPING MA
SIWEN SUN
HUI HAO
CHUNPING XU
spellingShingle YUPING MA
SIWEN SUN
HUI HAO
CHUNPING XU
Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09
Anais da Academia Brasileira de Ciências
Penicillium janthinellum
poligalacturonase
purificação
caracterização
author_facet YUPING MA
SIWEN SUN
HUI HAO
CHUNPING XU
author_sort YUPING MA
title Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09
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
publisher Academia Brasileira de Ciências
series Anais da Academia Brasileira de Ciências
issn 1678-2690
publishDate 2016-01-01
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.
topic Penicillium janthinellum
poligalacturonase
purificação
caracterização
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000200479&lng=en&tlng=en
work_keys_str_mv AT yupingma productionpurificationandcharacterizationofanexopolygalacturonasefrompenicilliumjanthinellumsw09
AT siwensun productionpurificationandcharacterizationofanexopolygalacturonasefrompenicilliumjanthinellumsw09
AT huihao productionpurificationandcharacterizationofanexopolygalacturonasefrompenicilliumjanthinellumsw09
AT chunpingxu productionpurificationandcharacterizationofanexopolygalacturonasefrompenicilliumjanthinellumsw09
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