Produção e caracterização de α-amilase produzida por Rhizopus sp.
Autor(a) principal: | |
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Data de Publicação: | 1996 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://hdl.handle.net/11449/230711 |
Resumo: | A strain of Rhizopus sp. screened among more than 800 filamentous fungi showed great ability to produce a thermostable α-amylase by solid state fermentation. The best production was obtained with a bran moisture content of 40% when the enzyme activity reached 60 EU/g. of medium. During the purification procedures, a column of DEAE-Sephadex A-50 separated the enzyme in two fractions and the larger (85% of the total activity) showed optimum pH in a range from -4.0 to 5.6. Optimum temperature was found at 60-65° C and in this range no loss of activity was observed after 60 min. of treatment in pH 5,0. Its Km and Vm are, respectively, of 5.0 mg/ml of starch and 10,01 uMol of reducing sugar/min./mg. of protein. Its molecular weight was calculated in 64.000 by gel filtration in Sepbadex G-200. The dextrinization power of the enzyme was observed preferentialy on substrates compound by chains with higher ramifications, that is: amylopectin > starch > amylose. Other aspects of the enzyme pattern action are also discussed. |
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Produção e caracterização de α-amilase produzida por Rhizopus sp.Production and characterization of α-amilase from Rhizopus sp.A strain of Rhizopus sp. screened among more than 800 filamentous fungi showed great ability to produce a thermostable α-amylase by solid state fermentation. The best production was obtained with a bran moisture content of 40% when the enzyme activity reached 60 EU/g. of medium. During the purification procedures, a column of DEAE-Sephadex A-50 separated the enzyme in two fractions and the larger (85% of the total activity) showed optimum pH in a range from -4.0 to 5.6. Optimum temperature was found at 60-65° C and in this range no loss of activity was observed after 60 min. of treatment in pH 5,0. Its Km and Vm are, respectively, of 5.0 mg/ml of starch and 10,01 uMol of reducing sugar/min./mg. of protein. Its molecular weight was calculated in 64.000 by gel filtration in Sepbadex G-200. The dextrinization power of the enzyme was observed preferentialy on substrates compound by chains with higher ramifications, that is: amylopectin > starch > amylose. Other aspects of the enzyme pattern action are also discussed.Departamento de Ciências Biológicas Faculdade de Ciências e Letras Campus Universitário, Av. Dom Antonio, 2100, CEP 19.800-000 - Assis - SPFaculdade de Ciências e LetrasDe Souza, Elisângela LucioHoffmann, Erika H.E.Castilho, Vanessa M.De Lima, Viviane A.Bellini, Márcia Z.Vinícius D'Arcadia Cruz, M.Cruz, Rubens2022-04-29T08:41:47Z2022-04-29T08:41:47Z1996-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article831-839Arquivos de Biologia e Technologia, v. 39, n. 4, p. 831-839, 1996.0365-0979http://hdl.handle.net/11449/2307112-s2.0-0001035027Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporArquivos de Biologia e Technologiainfo:eu-repo/semantics/openAccess2024-06-13T17:38:32Zoai:repositorio.unesp.br:11449/230711Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T19:47:12.471465Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Produção e caracterização de α-amilase produzida por Rhizopus sp. Production and characterization of α-amilase from Rhizopus sp. |
title |
Produção e caracterização de α-amilase produzida por Rhizopus sp. |
spellingShingle |
Produção e caracterização de α-amilase produzida por Rhizopus sp. De Souza, Elisângela Lucio |
title_short |
Produção e caracterização de α-amilase produzida por Rhizopus sp. |
title_full |
Produção e caracterização de α-amilase produzida por Rhizopus sp. |
title_fullStr |
Produção e caracterização de α-amilase produzida por Rhizopus sp. |
title_full_unstemmed |
Produção e caracterização de α-amilase produzida por Rhizopus sp. |
title_sort |
Produção e caracterização de α-amilase produzida por Rhizopus sp. |
author |
De Souza, Elisângela Lucio |
author_facet |
De Souza, Elisângela Lucio Hoffmann, Erika H.E. Castilho, Vanessa M. De Lima, Viviane A. Bellini, Márcia Z. Vinícius D'Arcadia Cruz, M. Cruz, Rubens |
author_role |
author |
author2 |
Hoffmann, Erika H.E. Castilho, Vanessa M. De Lima, Viviane A. Bellini, Márcia Z. Vinícius D'Arcadia Cruz, M. Cruz, Rubens |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Faculdade de Ciências e Letras |
dc.contributor.author.fl_str_mv |
De Souza, Elisângela Lucio Hoffmann, Erika H.E. Castilho, Vanessa M. De Lima, Viviane A. Bellini, Márcia Z. Vinícius D'Arcadia Cruz, M. Cruz, Rubens |
description |
A strain of Rhizopus sp. screened among more than 800 filamentous fungi showed great ability to produce a thermostable α-amylase by solid state fermentation. The best production was obtained with a bran moisture content of 40% when the enzyme activity reached 60 EU/g. of medium. During the purification procedures, a column of DEAE-Sephadex A-50 separated the enzyme in two fractions and the larger (85% of the total activity) showed optimum pH in a range from -4.0 to 5.6. Optimum temperature was found at 60-65° C and in this range no loss of activity was observed after 60 min. of treatment in pH 5,0. Its Km and Vm are, respectively, of 5.0 mg/ml of starch and 10,01 uMol of reducing sugar/min./mg. of protein. Its molecular weight was calculated in 64.000 by gel filtration in Sepbadex G-200. The dextrinization power of the enzyme was observed preferentialy on substrates compound by chains with higher ramifications, that is: amylopectin > starch > amylose. Other aspects of the enzyme pattern action are also discussed. |
publishDate |
1996 |
dc.date.none.fl_str_mv |
1996-12-01 2022-04-29T08:41:47Z 2022-04-29T08:41:47Z |
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 |
Arquivos de Biologia e Technologia, v. 39, n. 4, p. 831-839, 1996. 0365-0979 http://hdl.handle.net/11449/230711 2-s2.0-0001035027 |
identifier_str_mv |
Arquivos de Biologia e Technologia, v. 39, n. 4, p. 831-839, 1996. 0365-0979 2-s2.0-0001035027 |
url |
http://hdl.handle.net/11449/230711 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
Arquivos de Biologia e Technologia |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
831-839 |
dc.source.none.fl_str_mv |
Scopus 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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1808129118176280576 |