Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp.
Autor(a) principal: | |
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Data de Publicação: | 1983 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1007/BF01386502 http://www.locus.ufv.br/handle/123456789/22925 |
Resumo: | The beta-glucosidase of aHumicola sp. is partly characterized. The pH and temperature optima, thermal stability and Michaelis constants with p-nitrophenyl-beta-D-glucoside (PNPG) substrate suggest the existance of at least one extracellular and one intracellular enzyme. The extracellular activity is substantially more than that produced byTrichoderma reesei QM 9414. |
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2145 |
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Araujo, E. F.Barros, E. G.Caldas, R. A.Silva, D. O.2019-01-07T14:37:04Z2019-01-07T14:37:04Z1983-111573-6776https://doi.org/10.1007/BF01386502http://www.locus.ufv.br/handle/123456789/22925The beta-glucosidase of aHumicola sp. is partly characterized. The pH and temperature optima, thermal stability and Michaelis constants with p-nitrophenyl-beta-D-glucoside (PNPG) substrate suggest the existance of at least one extracellular and one intracellular enzyme. The extracellular activity is substantially more than that produced byTrichoderma reesei QM 9414.engBiotechnology LettersVolume 5, Issue 11, p. 781–784, November 1983Kluwer Academic Publishersinfo:eu-repo/semantics/openAccessEnzymeThermal stabilityIntracellular enzymeHumicolaExtracellular activityBeta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp.info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf218792https://locus.ufv.br//bitstream/123456789/22925/1/artigo.pdf13388ec1d6b07b1fbf82d7a5d6d66bb7MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/22925/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/229252019-01-07 11:42:10.687oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452019-01-07T14:42:10LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
title |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
spellingShingle |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. Araujo, E. F. Enzyme Thermal stability Intracellular enzyme Humicola Extracellular activity |
title_short |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
title_full |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
title_fullStr |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
title_full_unstemmed |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
title_sort |
Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. |
author |
Araujo, E. F. |
author_facet |
Araujo, E. F. Barros, E. G. Caldas, R. A. Silva, D. O. |
author_role |
author |
author2 |
Barros, E. G. Caldas, R. A. Silva, D. O. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Araujo, E. F. Barros, E. G. Caldas, R. A. Silva, D. O. |
dc.subject.pt-BR.fl_str_mv |
Enzyme Thermal stability Intracellular enzyme Humicola Extracellular activity |
topic |
Enzyme Thermal stability Intracellular enzyme Humicola Extracellular activity |
description |
The beta-glucosidase of aHumicola sp. is partly characterized. The pH and temperature optima, thermal stability and Michaelis constants with p-nitrophenyl-beta-D-glucoside (PNPG) substrate suggest the existance of at least one extracellular and one intracellular enzyme. The extracellular activity is substantially more than that produced byTrichoderma reesei QM 9414. |
publishDate |
1983 |
dc.date.issued.fl_str_mv |
1983-11 |
dc.date.accessioned.fl_str_mv |
2019-01-07T14:37:04Z |
dc.date.available.fl_str_mv |
2019-01-07T14:37:04Z |
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 |
https://doi.org/10.1007/BF01386502 http://www.locus.ufv.br/handle/123456789/22925 |
dc.identifier.issn.none.fl_str_mv |
1573-6776 |
identifier_str_mv |
1573-6776 |
url |
https://doi.org/10.1007/BF01386502 http://www.locus.ufv.br/handle/123456789/22925 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
Volume 5, Issue 11, p. 781–784, November 1983 |
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Kluwer Academic Publishers info:eu-repo/semantics/openAccess |
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Kluwer Academic Publishers |
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openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
Biotechnology Letters |
publisher.none.fl_str_mv |
Biotechnology Letters |
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Universidade Federal de Viçosa (UFV) |
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UFV |
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LOCUS Repositório Institucional da UFV |
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LOCUS Repositório Institucional da UFV |
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