Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Research, Society and Development |
Texto Completo: | https://rsdjournal.org/index.php/rsd/article/view/4810 |
Resumo: | Amylases have the ability to catalyze the α-1,4 binding of starch by releasing glucose and dextrin, with prominence in several industrial fields. The research sought to characterize the enzyme amylase obtained from the fungus Rhizopus microsporus var. oligosporus, through the Doehlert methodology, evaluating the behavior of the enzyme in the face of variations in pH and temperature. The production of amylase occurred with the use of starch as an inducer, and the characterization was carried out using the response surface methodology, with pH analysis at 5 levels (3.0, 4.0, 5.0, 6.0 and 7.0) and temperature in 3 levels (30, 50 and 70°C). The evaluation of the amylase thermostability occurred at 60, 70 and 80ºC. The application of the experimental model indicated that the amylase obtained from R. microsporus var. oligosporus shows better catalytic development at temperatures between 40ºC and 55ºC and pH between 2.5 and 3.2. The evaluation of thermostability indicated that the increase in temperature negatively influences the catalytic activity of amylase. The experimental model led to the understanding of the conditions favorable to the production of amylases from R. microsporus var. oligosporus. |
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Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporusProducción y caracterización de la amilasa obtenida de Rhizopus microsporus var. oligosporusProdução e caracterização da amilase obtida de Rhizopus microsporus var. oligosporusBiocatalysisThermostabilityResponse Surface Methodology.BiocatáliseTermoestabilidadeMetodologia de Superfície de Resposta.BiocatálisisTermoestabilidadMetodología de la Superficie de Respuesta.Amylases have the ability to catalyze the α-1,4 binding of starch by releasing glucose and dextrin, with prominence in several industrial fields. The research sought to characterize the enzyme amylase obtained from the fungus Rhizopus microsporus var. oligosporus, through the Doehlert methodology, evaluating the behavior of the enzyme in the face of variations in pH and temperature. The production of amylase occurred with the use of starch as an inducer, and the characterization was carried out using the response surface methodology, with pH analysis at 5 levels (3.0, 4.0, 5.0, 6.0 and 7.0) and temperature in 3 levels (30, 50 and 70°C). The evaluation of the amylase thermostability occurred at 60, 70 and 80ºC. The application of the experimental model indicated that the amylase obtained from R. microsporus var. oligosporus shows better catalytic development at temperatures between 40ºC and 55ºC and pH between 2.5 and 3.2. The evaluation of thermostability indicated that the increase in temperature negatively influences the catalytic activity of amylase. The experimental model led to the understanding of the conditions favorable to the production of amylases from R. microsporus var. oligosporus.Las amilasas tienen la capacidad de catalizar la unión α-1,4 del almidón mediante la liberación de glucosa y dextrina, con prominencia en varios campos industriales. La investigación buscó caracterizar la enzima amilasa obtenida del hongo Rhizopus microsporus var. oligosporus, utilizando la metodología de Doehlert, evaluando el comportamiento de la enzima ante variaciones de pH y temperatura. La producción de amilasa se produjo con el uso de almidón como inductor, y la caracterización se realizó utilizando la metodología de superficie de respuesta, con análisis de pH a 5 niveles (3.0, 4.0, 5.0, 6.0 y 7.0) y temperatura en 3 niveles (30, 50 y 70 ° C). La evaluación de la termoestabilidad de la amilasa se realizó a 60, 70 y 80ºC. La aplicación del modelo experimental indicó que la amilasa obtenida de R. microsporus var. oligosporus muestra un mejor desarrollo catalítico a temperaturas entre 40ºC y 55ºC y pH entre 2.5 y 3.2. La evaluación de la termoestabilidad indicó que el aumento de la temperatura influye negativamente en la actividad catalítica de la amilasa. El modelo experimental condujo a la comprensión de las condiciones favorables para la producción de amilasas de R. microsporus var. Oligosporus.As amilases possuem a capacidade de catalisar a ligação α-1,4 do amido liberando glicose e dextrina, com destaque em diversos campos industriais. A pesquisa buscou caracterizar a enzima amilase obtida do fungo Rhizopus microsporus var. oligosporus, através da metodologia de Doehlert, avaliando o comportamento da enzima frente as variações de pH e temperatura. A produção da amilase ocorreu com a utilização do amido como indutor, e a caracterização foi realizada através da metodologia de superfície de resposta, com a análise do pH em 5 níveis (3,0, 4,0, 5,0, 6,0 e 7,0) e temperatura em 3 níveis (30, 50 e 70 °C). A avaliação da termoestabilidade da amilase ocorreu à 60, 70 e 80ºC. A aplicação do modelo experimental indicou que a amilase obtida de R. microsporus var. oligosporus apresenta melhor desenvolvimento catalítico em temperaturas entre 40ºC e 55ºC e pH entre 2,5 e 3,2. A avaliação da termoestabilidade indicou que o aumento da temperatura influencia negativamente na atividade catalítica da amilase. O modelo experimental conduziu à compreensão das condições favoráveis à produção de amilases de R. microsporus var. oligosporus.Research, Society and Development2020-06-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://rsdjournal.org/index.php/rsd/article/view/481010.33448/rsd-v9i7.4810Research, Society and Development; Vol. 9 No. 7; e694974810Research, Society and Development; Vol. 9 Núm. 7; e694974810Research, Society and Development; v. 9 n. 7; e6949748102525-3409reponame:Research, Society and Developmentinstname:Universidade Federal de Itajubá (UNIFEI)instacron:UNIFEIporhttps://rsdjournal.org/index.php/rsd/article/view/4810/4092Copyright (c) 2020 Igor Ribeiro Santos, Tátilla Putumujú Santana Mendes, Alana Caise dos Anjos Miranda, Danilo Nascimento Costa, Gabriel Macedo Figueroa, Vyvian Dias Miranda Soares, Gildomar Lima Valasques Junior, Pâmala Évelin Pires Cedroinfo:eu-repo/semantics/openAccessSantos, Igor RibeiroMendes, Tátilla Putumujú SantanaMiranda, Alana Caise dos AnjosCosta, Danilo NascimentoFigueroa, Gabriel MacedoSoares, Vyvian Dias MirandaValasques Junior, Gildomar LimaCedro, Pâmala Évelin Pires2020-08-20T18:05:03Zoai:ojs.pkp.sfu.ca:article/4810Revistahttps://rsdjournal.org/index.php/rsd/indexPUBhttps://rsdjournal.org/index.php/rsd/oairsd.articles@gmail.com2525-34092525-3409opendoar:2024-01-17T09:28:31.844074Research, Society and Development - Universidade Federal de Itajubá (UNIFEI)false |
dc.title.none.fl_str_mv |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus Producción y caracterización de la amilasa obtenida de Rhizopus microsporus var. oligosporus Produção e caracterização da amilase obtida de Rhizopus microsporus var. oligosporus |
title |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus |
spellingShingle |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus Santos, Igor Ribeiro Biocatalysis Thermostability Response Surface Methodology. Biocatálise Termoestabilidade Metodologia de Superfície de Resposta. Biocatálisis Termoestabilidad Metodología de la Superficie de Respuesta. |
title_short |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus |
title_full |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus |
title_fullStr |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus |
title_full_unstemmed |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus |
title_sort |
Production and characterization of amylase obtained from Rhizopus microsporus var. oligosporus |
author |
Santos, Igor Ribeiro |
author_facet |
Santos, Igor Ribeiro Mendes, Tátilla Putumujú Santana Miranda, Alana Caise dos Anjos Costa, Danilo Nascimento Figueroa, Gabriel Macedo Soares, Vyvian Dias Miranda Valasques Junior, Gildomar Lima Cedro, Pâmala Évelin Pires |
author_role |
author |
author2 |
Mendes, Tátilla Putumujú Santana Miranda, Alana Caise dos Anjos Costa, Danilo Nascimento Figueroa, Gabriel Macedo Soares, Vyvian Dias Miranda Valasques Junior, Gildomar Lima Cedro, Pâmala Évelin Pires |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Santos, Igor Ribeiro Mendes, Tátilla Putumujú Santana Miranda, Alana Caise dos Anjos Costa, Danilo Nascimento Figueroa, Gabriel Macedo Soares, Vyvian Dias Miranda Valasques Junior, Gildomar Lima Cedro, Pâmala Évelin Pires |
dc.subject.por.fl_str_mv |
Biocatalysis Thermostability Response Surface Methodology. Biocatálise Termoestabilidade Metodologia de Superfície de Resposta. Biocatálisis Termoestabilidad Metodología de la Superficie de Respuesta. |
topic |
Biocatalysis Thermostability Response Surface Methodology. Biocatálise Termoestabilidade Metodologia de Superfície de Resposta. Biocatálisis Termoestabilidad Metodología de la Superficie de Respuesta. |
description |
Amylases have the ability to catalyze the α-1,4 binding of starch by releasing glucose and dextrin, with prominence in several industrial fields. The research sought to characterize the enzyme amylase obtained from the fungus Rhizopus microsporus var. oligosporus, through the Doehlert methodology, evaluating the behavior of the enzyme in the face of variations in pH and temperature. The production of amylase occurred with the use of starch as an inducer, and the characterization was carried out using the response surface methodology, with pH analysis at 5 levels (3.0, 4.0, 5.0, 6.0 and 7.0) and temperature in 3 levels (30, 50 and 70°C). The evaluation of the amylase thermostability occurred at 60, 70 and 80ºC. The application of the experimental model indicated that the amylase obtained from R. microsporus var. oligosporus shows better catalytic development at temperatures between 40ºC and 55ºC and pH between 2.5 and 3.2. The evaluation of thermostability indicated that the increase in temperature negatively influences the catalytic activity of amylase. The experimental model led to the understanding of the conditions favorable to the production of amylases from R. microsporus var. oligosporus. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-06-04 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://rsdjournal.org/index.php/rsd/article/view/4810 10.33448/rsd-v9i7.4810 |
url |
https://rsdjournal.org/index.php/rsd/article/view/4810 |
identifier_str_mv |
10.33448/rsd-v9i7.4810 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
https://rsdjournal.org/index.php/rsd/article/view/4810/4092 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Research, Society and Development |
publisher.none.fl_str_mv |
Research, Society and Development |
dc.source.none.fl_str_mv |
Research, Society and Development; Vol. 9 No. 7; e694974810 Research, Society and Development; Vol. 9 Núm. 7; e694974810 Research, Society and Development; v. 9 n. 7; e694974810 2525-3409 reponame:Research, Society and Development instname:Universidade Federal de Itajubá (UNIFEI) instacron:UNIFEI |
instname_str |
Universidade Federal de Itajubá (UNIFEI) |
instacron_str |
UNIFEI |
institution |
UNIFEI |
reponame_str |
Research, Society and Development |
collection |
Research, Society and Development |
repository.name.fl_str_mv |
Research, Society and Development - Universidade Federal de Itajubá (UNIFEI) |
repository.mail.fl_str_mv |
rsd.articles@gmail.com |
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1797052815776940032 |