Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano
Autor(a) principal: | |
---|---|
Data de Publicação: | 2022 |
Tipo de documento: | Dissertação |
Idioma: | por |
Título da fonte: | Biblioteca Digital de Teses e Dissertações da UEFS |
Texto Completo: | http://tede2.uefs.br:8080/handle/tede/1504 |
Resumo: | Enzymes are versatile catalysts present in animal, plant and microorganism cells; they have several properties that make them attractive as catalysts in various bioprocesses. β-glucanases consist of a set of enzymes that act synergistically to degrade glucan, its potential is explored in the beverage industry to improve organoleptic characteristics of wines, in feed supplementation, in biological control and in the manufacture of detergents. The objective of this work was to evaluate and characterize the β-1,3-glucanase activity by the yeast Rhodotorula oryzicola cultivated in liquid medium. Response surface analysis was used to determine the most suitable pH and temperature parameters for enzymatic activity. Thermostability was studied at temperatures from 50 oC to 70 oC, in times ranging from 0 to 50 min. The influence of NaCl at concentrations from 0.2 to 1 M was evaluated. A centroid simplex mixture design was used in the study of enzyme stabilization by a mixture of preservatives composed of sodium chloride (SC), sodium benzoate (SB) and monosodium phosphate (MSP). The optimum conditions of enzymatic activity were obtained at 50oC and pH 8.0 with activity of 0.9601 μmol/min. After 30 minutes of incubation in 50, 60 oC and 70 oC enzymatic activity remained at 100%, 94.6% and 62.39%, respectively. The presence of NaCl increased enzymatic activity in all concentrations studied. In the study of preservatives, according to the response surface of the cubic model, the best result was obtained in the proportion of 20% sodium chloride, 70% sodium benzoate and 10% monosodium phosphate. The results show that yeast is capable of producing the enzyme β-1,3-glucanase and stabilizers have shown promise to maintain enzymatic stability in preparations. |
id |
UEFS_3c1889da1d67a6d0e0e0815f65d16139 |
---|---|
oai_identifier_str |
oai:tede2.uefs.br:8080:tede/1504 |
network_acronym_str |
UEFS |
network_name_str |
Biblioteca Digital de Teses e Dissertações da UEFS |
repository_id_str |
|
spelling |
Assis, Sandra Aparecida de19540160855http://lattes.cnpq.br/8688783103064480Benevides, Raquel Guimarães00392337312http://lattes.cnpq.br/763311523737920902950096590http://lattes.cnpq.br/7152851872022376Pereira, Manuela Oliveira2023-08-09T13:00:36Z2022-02-25PEREIRA, Manuela Oliveira. Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano. 2022. 79 f. Dissertação (Mestrado Acadêmico em Biotecnologia) - Universidade Estadual de Feira de Santana, Feira de Santana.http://tede2.uefs.br:8080/handle/tede/1504Enzymes are versatile catalysts present in animal, plant and microorganism cells; they have several properties that make them attractive as catalysts in various bioprocesses. β-glucanases consist of a set of enzymes that act synergistically to degrade glucan, its potential is explored in the beverage industry to improve organoleptic characteristics of wines, in feed supplementation, in biological control and in the manufacture of detergents. The objective of this work was to evaluate and characterize the β-1,3-glucanase activity by the yeast Rhodotorula oryzicola cultivated in liquid medium. Response surface analysis was used to determine the most suitable pH and temperature parameters for enzymatic activity. Thermostability was studied at temperatures from 50 oC to 70 oC, in times ranging from 0 to 50 min. The influence of NaCl at concentrations from 0.2 to 1 M was evaluated. A centroid simplex mixture design was used in the study of enzyme stabilization by a mixture of preservatives composed of sodium chloride (SC), sodium benzoate (SB) and monosodium phosphate (MSP). The optimum conditions of enzymatic activity were obtained at 50oC and pH 8.0 with activity of 0.9601 μmol/min. After 30 minutes of incubation in 50, 60 oC and 70 oC enzymatic activity remained at 100%, 94.6% and 62.39%, respectively. The presence of NaCl increased enzymatic activity in all concentrations studied. In the study of preservatives, according to the response surface of the cubic model, the best result was obtained in the proportion of 20% sodium chloride, 70% sodium benzoate and 10% monosodium phosphate. The results show that yeast is capable of producing the enzyme β-1,3-glucanase and stabilizers have shown promise to maintain enzymatic stability in preparations.As enzimas são catalisadores versáteis presentes em células de animais, vegetais e micro-organismos, apresentam várias propriedades que as tornam atrativas como catalisadores em diversos bioprocessos. As β-glucanases consistem em um conjunto de enzimas que atuam sinergicamente para degradar glucana, seu potencial é explorado na indústria de bebidas para melhorar características organolépticas de vinhos, na suplementação de rações, no controle biológico e na fabricação de detergentes. O objetivo do trabalho foi produzir e caracterizar a enzimaβ-1,3-glucanase produzida pela levedura Rhodotorula oryzicola cultivada em meio líquido. A análise de superfície de resposta foi utilizada para determinar os parâmetros de pH e temperatura mais adequados para a atividade enzimática. A termoestabilidade foi estudada em temperaturas de 50 oC a 70 oC, em tempos variando de 0 a 50 min. Foi avaliada a influência de NaCl nas concentrações de 0,2 a 1 M. Um planejamento de mistura simplex centróide foi usado no estudo de estabilização da enzima por uma mistura de conservantes composta por cloreto de sódio (SC), benzoato de sódio (SB) e fosfato monossódico (MSP). As condições ótimas de atividade enzimática foram obtidas na temperatura de 50oC e pH 8,0 com atividade de 0,9601 µmol/min. Após 30 minutos de incubação em 50, 60 oC e 70 oC atividade enzimática manteve-se em 100%, 94,6% e 62,39%, respectivamente. A presença de NaCl elevou a atividade enzimática em todas as concentrações estudadas. No estudo de conservantes, de acordo com superfície de resposta do modelo cúbico, o melhor resultado foi obtido na proporção de 20% de cloreto de sódio, 70% de benzoato de sódio e 10% de fosfato monossódio. Os resultados mostram que a levedura é capaz de produzir a enzima β-1,3-glucanase e os estabilizantes se mostraram promissores para manter a estabilidade enzimática em preparações.Submitted by Amanda Ponce (aponce@uefs.br) on 2023-08-09T13:00:36Z No. of bitstreams: 1 Dissertacao_Manuela_Oliveira.versao_Final.pdf: 2074174 bytes, checksum: 15b2dba44696ad91ae3a5d8c225a0286 (MD5)Made available in DSpace on 2023-08-09T13:00:36Z (GMT). No. of bitstreams: 1 Dissertacao_Manuela_Oliveira.versao_Final.pdf: 2074174 bytes, checksum: 15b2dba44696ad91ae3a5d8c225a0286 (MD5) Previous issue date: 2022-02-25Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESapplication/pdfporUniversidade Estadual de Feira de SantanaMestrado Acadêmico em BiotecnologiaUEFSBrasilDEPARTAMENTO DE CIÊNCIAS BIOLÓGICASLevedurasGlucanaseLaminarinaOtimizaçãoYeastsGlucanaseLaminarinOptimizationCIENCIAS BIOLOGICAS::BIOLOGIA GERALCIENCIAS BIOLOGICAS::MICROBIOLOGIABIOQUIMICA::ENZIMOLOGIAProdução de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baianoinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesis7701973706309601282600600600600600600-6971480722008537872-1634559385931244697-3854583469976220812-37137987929845631622075167498588264571info:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UEFSinstname:Universidade Estadual de Feira de Santana (UEFS)instacron:UEFSORIGINALDissertacao_Manuela_Oliveira.versao_Final.pdfDissertacao_Manuela_Oliveira.versao_Final.pdfapplication/pdf2074174http://tede2.uefs.br:8080/bitstream/tede/1504/2/Dissertacao_Manuela_Oliveira.versao_Final.pdf15b2dba44696ad91ae3a5d8c225a0286MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-82165http://tede2.uefs.br:8080/bitstream/tede/1504/1/license.txtbd3efa91386c1718a7f26a329fdcb468MD51tede/15042023-08-09 10:00:36.431oai:tede2.uefs.br:8080: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Biblioteca Digital de Teses e Dissertaçõeshttp://tede2.uefs.br:8080/PUBhttp://tede2.uefs.br:8080/oai/requestbcuefs@uefs.br|| bcref@uefs.br||bcuefs@uefs.bropendoar:2023-08-09T13:00:36Biblioteca Digital de Teses e Dissertações da UEFS - Universidade Estadual de Feira de Santana (UEFS)false |
dc.title.por.fl_str_mv |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
title |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
spellingShingle |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano Pereira, Manuela Oliveira Leveduras Glucanase Laminarina Otimização Yeasts Glucanase Laminarin Optimization CIENCIAS BIOLOGICAS::BIOLOGIA GERAL CIENCIAS BIOLOGICAS::MICROBIOLOGIA BIOQUIMICA::ENZIMOLOGIA |
title_short |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
title_full |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
title_fullStr |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
title_full_unstemmed |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
title_sort |
Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano |
author |
Pereira, Manuela Oliveira |
author_facet |
Pereira, Manuela Oliveira |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Assis, Sandra Aparecida de |
dc.contributor.advisor1ID.fl_str_mv |
19540160855 |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/8688783103064480 |
dc.contributor.advisor-co1.fl_str_mv |
Benevides, Raquel Guimarães |
dc.contributor.advisor-co1ID.fl_str_mv |
00392337312 |
dc.contributor.advisor-co1Lattes.fl_str_mv |
http://lattes.cnpq.br/7633115237379209 |
dc.contributor.authorID.fl_str_mv |
02950096590 |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/7152851872022376 |
dc.contributor.author.fl_str_mv |
Pereira, Manuela Oliveira |
contributor_str_mv |
Assis, Sandra Aparecida de Benevides, Raquel Guimarães |
dc.subject.por.fl_str_mv |
Leveduras Glucanase Laminarina Otimização |
topic |
Leveduras Glucanase Laminarina Otimização Yeasts Glucanase Laminarin Optimization CIENCIAS BIOLOGICAS::BIOLOGIA GERAL CIENCIAS BIOLOGICAS::MICROBIOLOGIA BIOQUIMICA::ENZIMOLOGIA |
dc.subject.eng.fl_str_mv |
Yeasts Glucanase Laminarin Optimization |
dc.subject.cnpq.fl_str_mv |
CIENCIAS BIOLOGICAS::BIOLOGIA GERAL CIENCIAS BIOLOGICAS::MICROBIOLOGIA BIOQUIMICA::ENZIMOLOGIA |
description |
Enzymes are versatile catalysts present in animal, plant and microorganism cells; they have several properties that make them attractive as catalysts in various bioprocesses. β-glucanases consist of a set of enzymes that act synergistically to degrade glucan, its potential is explored in the beverage industry to improve organoleptic characteristics of wines, in feed supplementation, in biological control and in the manufacture of detergents. The objective of this work was to evaluate and characterize the β-1,3-glucanase activity by the yeast Rhodotorula oryzicola cultivated in liquid medium. Response surface analysis was used to determine the most suitable pH and temperature parameters for enzymatic activity. Thermostability was studied at temperatures from 50 oC to 70 oC, in times ranging from 0 to 50 min. The influence of NaCl at concentrations from 0.2 to 1 M was evaluated. A centroid simplex mixture design was used in the study of enzyme stabilization by a mixture of preservatives composed of sodium chloride (SC), sodium benzoate (SB) and monosodium phosphate (MSP). The optimum conditions of enzymatic activity were obtained at 50oC and pH 8.0 with activity of 0.9601 μmol/min. After 30 minutes of incubation in 50, 60 oC and 70 oC enzymatic activity remained at 100%, 94.6% and 62.39%, respectively. The presence of NaCl increased enzymatic activity in all concentrations studied. In the study of preservatives, according to the response surface of the cubic model, the best result was obtained in the proportion of 20% sodium chloride, 70% sodium benzoate and 10% monosodium phosphate. The results show that yeast is capable of producing the enzyme β-1,3-glucanase and stabilizers have shown promise to maintain enzymatic stability in preparations. |
publishDate |
2022 |
dc.date.issued.fl_str_mv |
2022-02-25 |
dc.date.accessioned.fl_str_mv |
2023-08-09T13:00:36Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
PEREIRA, Manuela Oliveira. Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano. 2022. 79 f. Dissertação (Mestrado Acadêmico em Biotecnologia) - Universidade Estadual de Feira de Santana, Feira de Santana. |
dc.identifier.uri.fl_str_mv |
http://tede2.uefs.br:8080/handle/tede/1504 |
identifier_str_mv |
PEREIRA, Manuela Oliveira. Produção de β-1,3-glunacase por Rhodotorula oryzicola isolada do semiárido baiano. 2022. 79 f. Dissertação (Mestrado Acadêmico em Biotecnologia) - Universidade Estadual de Feira de Santana, Feira de Santana. |
url |
http://tede2.uefs.br:8080/handle/tede/1504 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.program.fl_str_mv |
7701973706309601282 |
dc.relation.confidence.fl_str_mv |
600 600 600 600 600 600 |
dc.relation.department.fl_str_mv |
-6971480722008537872 |
dc.relation.cnpq.fl_str_mv |
-1634559385931244697 -3854583469976220812 -3713798792984563162 |
dc.relation.sponsorship.fl_str_mv |
2075167498588264571 |
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 |
Universidade Estadual de Feira de Santana |
dc.publisher.program.fl_str_mv |
Mestrado Acadêmico em Biotecnologia |
dc.publisher.initials.fl_str_mv |
UEFS |
dc.publisher.country.fl_str_mv |
Brasil |
dc.publisher.department.fl_str_mv |
DEPARTAMENTO DE CIÊNCIAS BIOLÓGICAS |
publisher.none.fl_str_mv |
Universidade Estadual de Feira de Santana |
dc.source.none.fl_str_mv |
reponame:Biblioteca Digital de Teses e Dissertações da UEFS instname:Universidade Estadual de Feira de Santana (UEFS) instacron:UEFS |
instname_str |
Universidade Estadual de Feira de Santana (UEFS) |
instacron_str |
UEFS |
institution |
UEFS |
reponame_str |
Biblioteca Digital de Teses e Dissertações da UEFS |
collection |
Biblioteca Digital de Teses e Dissertações da UEFS |
bitstream.url.fl_str_mv |
http://tede2.uefs.br:8080/bitstream/tede/1504/2/Dissertacao_Manuela_Oliveira.versao_Final.pdf http://tede2.uefs.br:8080/bitstream/tede/1504/1/license.txt |
bitstream.checksum.fl_str_mv |
15b2dba44696ad91ae3a5d8c225a0286 bd3efa91386c1718a7f26a329fdcb468 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 |
repository.name.fl_str_mv |
Biblioteca Digital de Teses e Dissertações da UEFS - Universidade Estadual de Feira de Santana (UEFS) |
repository.mail.fl_str_mv |
bcuefs@uefs.br|| bcref@uefs.br||bcuefs@uefs.br |
_version_ |
1809288785761927168 |