Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola
Autor(a) principal: | |
---|---|
Data de Publicação: | 2020 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10437/12147 |
Resumo: | The protease was produced extracellularly in submerged fermentation by the yeast Rhodotorula oryzicola using different sources of nitrogen and maximum activity (6.54 × 10−3 U/mg) was obtained in medium containing 2% casein (w/v). Purification of the protease by gel filtration chromatography resulted in a 3.07-fold increase of specific protease activity. The optimal pH and temperature for enzyme activity were 6.51 and 63.04 °C, respectively. Incubation in the presence of some salts enhanced enzyme activity, which peaked under 0.01 M BaCl2. The enzyme retained about 90% of enzymatic activity at temperatures 50–60 °C. The commercially available enzyme carriers evaluated, silica gel, Celite 545, and chitosan effectively immobilized the protease. The enzyme immobilized in Celite 545 retained 73.53% of the initial activity after 15 reuse cycles. These results are quite promising for large-scale production and immobilization of protease from R. oryzicola, as the high operational stability of the immobilized enzyme lowers production costs in biotechnological applications that require high enzymatic activity and stability under high temperatures. |
id |
RCAP_2ad0fb0c684e858c1601ff859ad71ae3 |
---|---|
oai_identifier_str |
oai:recil.ensinolusofona.pt:10437/12147 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicolaBIOTECNOLOGIABIOQUÍMICAENZIMOLOGIABIOTECHNOLOGYBIOCHEMISTRYENZYMOLOGYThe protease was produced extracellularly in submerged fermentation by the yeast Rhodotorula oryzicola using different sources of nitrogen and maximum activity (6.54 × 10−3 U/mg) was obtained in medium containing 2% casein (w/v). Purification of the protease by gel filtration chromatography resulted in a 3.07-fold increase of specific protease activity. The optimal pH and temperature for enzyme activity were 6.51 and 63.04 °C, respectively. Incubation in the presence of some salts enhanced enzyme activity, which peaked under 0.01 M BaCl2. The enzyme retained about 90% of enzymatic activity at temperatures 50–60 °C. The commercially available enzyme carriers evaluated, silica gel, Celite 545, and chitosan effectively immobilized the protease. The enzyme immobilized in Celite 545 retained 73.53% of the initial activity after 15 reuse cycles. These results are quite promising for large-scale production and immobilization of protease from R. oryzicola, as the high operational stability of the immobilized enzyme lowers production costs in biotechnological applications that require high enzymatic activity and stability under high temperatures.Wiley2021-09-06T11:50:49Z2020-01-01T00:00:00Z2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10437/12147eng10.1002/bab.2023Oliveira, Juliana Mota deFernandes, Pedro Carlos de BarrosBenevides, Raquel GuimarãesAssis, Sandra Aparecida deinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-03-09T14:06:06Zoai:recil.ensinolusofona.pt:10437/12147Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T17:13:43.243644Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
title |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
spellingShingle |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola Oliveira, Juliana Mota de BIOTECNOLOGIA BIOQUÍMICA ENZIMOLOGIA BIOTECHNOLOGY BIOCHEMISTRY ENZYMOLOGY |
title_short |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
title_full |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
title_fullStr |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
title_full_unstemmed |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
title_sort |
Production, characterization, and immobilization of protease from the yeast Rhodotorula oryzicola |
author |
Oliveira, Juliana Mota de |
author_facet |
Oliveira, Juliana Mota de Fernandes, Pedro Carlos de Barros Benevides, Raquel Guimarães Assis, Sandra Aparecida de |
author_role |
author |
author2 |
Fernandes, Pedro Carlos de Barros Benevides, Raquel Guimarães Assis, Sandra Aparecida de |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Oliveira, Juliana Mota de Fernandes, Pedro Carlos de Barros Benevides, Raquel Guimarães Assis, Sandra Aparecida de |
dc.subject.por.fl_str_mv |
BIOTECNOLOGIA BIOQUÍMICA ENZIMOLOGIA BIOTECHNOLOGY BIOCHEMISTRY ENZYMOLOGY |
topic |
BIOTECNOLOGIA BIOQUÍMICA ENZIMOLOGIA BIOTECHNOLOGY BIOCHEMISTRY ENZYMOLOGY |
description |
The protease was produced extracellularly in submerged fermentation by the yeast Rhodotorula oryzicola using different sources of nitrogen and maximum activity (6.54 × 10−3 U/mg) was obtained in medium containing 2% casein (w/v). Purification of the protease by gel filtration chromatography resulted in a 3.07-fold increase of specific protease activity. The optimal pH and temperature for enzyme activity were 6.51 and 63.04 °C, respectively. Incubation in the presence of some salts enhanced enzyme activity, which peaked under 0.01 M BaCl2. The enzyme retained about 90% of enzymatic activity at temperatures 50–60 °C. The commercially available enzyme carriers evaluated, silica gel, Celite 545, and chitosan effectively immobilized the protease. The enzyme immobilized in Celite 545 retained 73.53% of the initial activity after 15 reuse cycles. These results are quite promising for large-scale production and immobilization of protease from R. oryzicola, as the high operational stability of the immobilized enzyme lowers production costs in biotechnological applications that require high enzymatic activity and stability under high temperatures. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-01-01T00:00:00Z 2020 2021-09-06T11:50:49Z |
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://hdl.handle.net/10437/12147 |
url |
http://hdl.handle.net/10437/12147 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1002/bab.2023 |
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 |
Wiley |
publisher.none.fl_str_mv |
Wiley |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
|
_version_ |
1799131234114207744 |