Immobilization and Characterization of L-Asparaginase over Carbon Xerogels

Detalhes bibliográficos
Autor(a) principal: Barros, Rita A. M.
Data de Publicação: 2022
Outros Autores: Cristóvão, Raquel O., Carabineiro, Sónia A. C., Neves, Márcia C., Freire, Mara G., Faria, Joaquim L., Santos-Ebinuma, Valéria C., Tavares, Ana P. M., Silva, Cláudia G.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/139991
Resumo: UIDP/ 50020/2020 POCI-01-0145-FEDER-031268 no. 312463/2021-9 LA/P/0006/2020 FAPESP (2018/06908-8) CEECIND/2020/01867
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spelling Immobilization and Characterization of L-Asparaginase over Carbon Xerogelscarbon xerogelscentral composite designenzyme immobilizationL-asparaginasephysical adsorptionBiochemistryBiotechnologyBioengineeringBiomedical EngineeringApplied Microbiology and BiotechnologyUIDP/ 50020/2020 POCI-01-0145-FEDER-031268 no. 312463/2021-9 LA/P/0006/2020 FAPESP (2018/06908-8) CEECIND/2020/01867L-asparaginase (ASNase) is an aminohydrolase currently used in the pharmaceutical and food industries. Enzyme immobilization is an exciting option for both applications, allowing for a more straightforward recovery and increased stability. High surface area and customizable porosity make carbon xerogels (CXs) promising materials for ASNase immobilization. This work describes the influence of contact time, pH, and ASNase concentration on the immobilization yield (IY) and relative recovered activity (RRA) using the Central Composite Design methodology. The most promising results were obtained using CX with an average pore size of 4 nm (CX-4), reaching IY and RRA of 100%. At the optimal conditions (contact time 49 min, pH 6.73, and [ASNase] 0.26 mg·mL−1), the ASNase-CXs biocomposite was characterized and evaluated in terms of kinetic properties and operational, thermal, and pH stabilities. The immobilized ASNase onto CX-4 retained 71% of its original activity after six continuous reaction cycles, showed good thermal stability at 37 °C (RRA of 91% after 90 min), and was able to adapt to both acidic and alkaline environments. Finally, the results indicated a 3.9-fold increase in the immobilized ASNase affinity for the substrate, confirming the potential of CXs as a support for ASNase and as a cost-effective tool for subsequent use in the therapeutic and food sectors.LAQV@REQUIMTEDQ - Departamento de QuímicaRUNBarros, Rita A. M.Cristóvão, Raquel O.Carabineiro, Sónia A. C.Neves, Márcia C.Freire, Mara G.Faria, Joaquim L.Santos-Ebinuma, Valéria C.Tavares, Ana P. M.Silva, Cláudia G.2022-06-14T22:23:58Z2022-062022-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/139991eng2673-6284PURE: 43985842https://doi.org/10.3390/biotech11020010info: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:RCAAP2024-03-11T05:17:05Zoai:run.unl.pt:10362/139991Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:49:31.696489Repositório 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 Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
title Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
spellingShingle Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
Barros, Rita A. M.
carbon xerogels
central composite design
enzyme immobilization
L-asparaginase
physical adsorption
Biochemistry
Biotechnology
Bioengineering
Biomedical Engineering
Applied Microbiology and Biotechnology
title_short Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
title_full Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
title_fullStr Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
title_full_unstemmed Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
title_sort Immobilization and Characterization of L-Asparaginase over Carbon Xerogels
author Barros, Rita A. M.
author_facet Barros, Rita A. M.
Cristóvão, Raquel O.
Carabineiro, Sónia A. C.
Neves, Márcia C.
Freire, Mara G.
Faria, Joaquim L.
Santos-Ebinuma, Valéria C.
Tavares, Ana P. M.
Silva, Cláudia G.
author_role author
author2 Cristóvão, Raquel O.
Carabineiro, Sónia A. C.
Neves, Márcia C.
Freire, Mara G.
Faria, Joaquim L.
Santos-Ebinuma, Valéria C.
Tavares, Ana P. M.
Silva, Cláudia G.
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv LAQV@REQUIMTE
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Barros, Rita A. M.
Cristóvão, Raquel O.
Carabineiro, Sónia A. C.
Neves, Márcia C.
Freire, Mara G.
Faria, Joaquim L.
Santos-Ebinuma, Valéria C.
Tavares, Ana P. M.
Silva, Cláudia G.
dc.subject.por.fl_str_mv carbon xerogels
central composite design
enzyme immobilization
L-asparaginase
physical adsorption
Biochemistry
Biotechnology
Bioengineering
Biomedical Engineering
Applied Microbiology and Biotechnology
topic carbon xerogels
central composite design
enzyme immobilization
L-asparaginase
physical adsorption
Biochemistry
Biotechnology
Bioengineering
Biomedical Engineering
Applied Microbiology and Biotechnology
description UIDP/ 50020/2020 POCI-01-0145-FEDER-031268 no. 312463/2021-9 LA/P/0006/2020 FAPESP (2018/06908-8) CEECIND/2020/01867
publishDate 2022
dc.date.none.fl_str_mv 2022-06-14T22:23:58Z
2022-06
2022-06-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/139991
url http://hdl.handle.net/10362/139991
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2673-6284
PURE: 43985842
https://doi.org/10.3390/biotech11020010
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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instacron:RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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