Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://www.hindawi.com/journals/er/2013/438645/ http://hdl.handle.net/11449/122575 |
Resumo: | Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was carried out in culture media containing sugar cane bagasse and orange bagasse in proportions of 30% and 70% (w/w) at 45°C for 4 days. PG obtained was purified by gel filtration and ion-exchange chromatography. The highest activity was found between pH 4.5 and 5.5, and the enzyme preserved more than 80% of its activity at pH values between 5.0 and 6.5. At pH values between 3.0 and 4.5, PG retained about 73% of the original activity, whereas at pH 10.0 it remained around 44%. The optimum temperature was 60–65°C. The enzyme was completely stable when incubated for 1 hour at 50°C. At 55°C and 60°C, the activity decreased 55% and 90%, respectively. The apparent molecular weight was 29.3 kDa, Km of 1.58 mg/mL and Vmax of 1553.1μmol/min/mg. The presence of Zn+2, Mn+2, and Hg+2 inhibited 59%, 77%, and 100% of enzyme activity, respectively. The hydrolysis product suggests that polygalacturonase was shown to be an endo/exoenzyme. |
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Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentationPolygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was carried out in culture media containing sugar cane bagasse and orange bagasse in proportions of 30% and 70% (w/w) at 45°C for 4 days. PG obtained was purified by gel filtration and ion-exchange chromatography. The highest activity was found between pH 4.5 and 5.5, and the enzyme preserved more than 80% of its activity at pH values between 5.0 and 6.5. At pH values between 3.0 and 4.5, PG retained about 73% of the original activity, whereas at pH 10.0 it remained around 44%. The optimum temperature was 60–65°C. The enzyme was completely stable when incubated for 1 hour at 50°C. At 55°C and 60°C, the activity decreased 55% and 90%, respectively. The apparent molecular weight was 29.3 kDa, Km of 1.58 mg/mL and Vmax of 1553.1μmol/min/mg. The presence of Zn+2, Mn+2, and Hg+2 inhibited 59%, 77%, and 100% of enzyme activity, respectively. The hydrolysis product suggests that polygalacturonase was shown to be an endo/exoenzyme.Universidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Química e Ciências Ambientais, Instituto de Biociências Letras e Ciências Exatas de São José do Rio Preto, Sao Jose do Rio Preto, Rua Cristovão Colombo, 2265, Jardim Nazareth, CEP 15054-000, SP, BrasilUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Química e Ciências Ambientais, Instituto de Biociências Letras e Ciências Exatas de São José do Rio Preto, Sao Jose do Rio Preto, Rua Cristovão Colombo, 2265, Jardim Nazareth, CEP 15054-000, SP, BrasilLaboratório de Microbiologia, Universidade do Estado de Minas Gerais (UEMG), Avenida Prof. Mario Palmerio 1000, 38200-000 Frutal, MG, BrazilFaculdade de Ciências Biológicas e Ambientais (FCBA), Universidade Federal da Grande Dourados (UFGD), Rodovia Dourados-Itahum, Km 12, 79804-970 Dourados, MS, BrazilUniversidade Estadual Paulista (Unesp)Martins, Eduardo da SilvaLeite, Rodrigo Simões RibeiroSilva, Roberto da [UNESP]Gomes, Eleni [UNESP]2015-04-27T11:55:52Z2015-04-27T11:55:52Z2013info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1-7application/pdfhttp://www.hindawi.com/journals/er/2013/438645/Enzyme Research, v. 2013, p. 1-7, 2013.2090-0406http://hdl.handle.net/11449/12257510.1155/2013/438645ISSN2090-0406-2013-2013-01-07.pdf94241756882065457091241742851920Currículo Lattesreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengEnzyme Research0,653info:eu-repo/semantics/openAccess2023-10-17T06:08:50Zoai:repositorio.unesp.br:11449/122575Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:11:38.300404Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
title |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
spellingShingle |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation Martins, Eduardo da Silva |
title_short |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
title_full |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
title_fullStr |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
title_full_unstemmed |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
title_sort |
Purification and properties of polygalacturonase produced by thermophilic fungus Thermoascus aurantiacus CBMAI-756 on solid-state fermentation |
author |
Martins, Eduardo da Silva |
author_facet |
Martins, Eduardo da Silva Leite, Rodrigo Simões Ribeiro Silva, Roberto da [UNESP] Gomes, Eleni [UNESP] |
author_role |
author |
author2 |
Leite, Rodrigo Simões Ribeiro Silva, Roberto da [UNESP] Gomes, Eleni [UNESP] |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Martins, Eduardo da Silva Leite, Rodrigo Simões Ribeiro Silva, Roberto da [UNESP] Gomes, Eleni [UNESP] |
description |
Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was carried out in culture media containing sugar cane bagasse and orange bagasse in proportions of 30% and 70% (w/w) at 45°C for 4 days. PG obtained was purified by gel filtration and ion-exchange chromatography. The highest activity was found between pH 4.5 and 5.5, and the enzyme preserved more than 80% of its activity at pH values between 5.0 and 6.5. At pH values between 3.0 and 4.5, PG retained about 73% of the original activity, whereas at pH 10.0 it remained around 44%. The optimum temperature was 60–65°C. The enzyme was completely stable when incubated for 1 hour at 50°C. At 55°C and 60°C, the activity decreased 55% and 90%, respectively. The apparent molecular weight was 29.3 kDa, Km of 1.58 mg/mL and Vmax of 1553.1μmol/min/mg. The presence of Zn+2, Mn+2, and Hg+2 inhibited 59%, 77%, and 100% of enzyme activity, respectively. The hydrolysis product suggests that polygalacturonase was shown to be an endo/exoenzyme. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 2015-04-27T11:55:52Z 2015-04-27T11:55:52Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.hindawi.com/journals/er/2013/438645/ Enzyme Research, v. 2013, p. 1-7, 2013. 2090-0406 http://hdl.handle.net/11449/122575 10.1155/2013/438645 ISSN2090-0406-2013-2013-01-07.pdf 9424175688206545 7091241742851920 |
url |
http://www.hindawi.com/journals/er/2013/438645/ http://hdl.handle.net/11449/122575 |
identifier_str_mv |
Enzyme Research, v. 2013, p. 1-7, 2013. 2090-0406 10.1155/2013/438645 ISSN2090-0406-2013-2013-01-07.pdf 9424175688206545 7091241742851920 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Enzyme Research 0,653 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
1-7 application/pdf |
dc.source.none.fl_str_mv |
Currículo Lattes reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1808128477728079872 |