Reutilization of the most stable coimmobilized enzyme using glutaraldehyde chemistry to produce a new combi-biocatalyst when the coimmobilized enzyme with a lower stability is inactivated (2024)
- Authors:
- USP affiliated authors: POLIZELI, MARIA DE LOURDES TEIXEIRA DE MORAES - FFCLRP ; ANDRADES, DIANDRA DE - FFCLRP
- Unidade: FFCLRP
- DOI: 10.1021/acssuschemeng.3c08231
- Subjects: ENZIMAS; CATALISADORES; DESINFETANTES; REAÇÕES QUÍMICAS
- Keywords: Enzyme coimmobilization; Dissimilar enzyme stabilities; Reuse of stable coimmobilized enzymes; Enzyme release from combi-biocatalysts
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 2024
- Source:
- Título: ACS Sustainable Chemistry & Engineering
- ISSN: 2168-0485
- Volume/Número/Paginação/Ano: v. 12, n. 17, p. 6564-6572, 2024
- Status:
- Artigo aberto em periódico híbrido (Hybrid Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
CARBALLARES, Diego et al. Reutilization of the most stable coimmobilized enzyme using glutaraldehyde chemistry to produce a new combi-biocatalyst when the coimmobilized enzyme with a lower stability is inactivated. ACS Sustainable Chemistry & Engineering, v. 12, n. 17, p. 6564-6572, 2024Tradução . . Disponível em: https://doi.org/10.1021/acssuschemeng.3c08231. Acesso em: 31 mar. 2026. -
APA
Carballares, D., Abellanas-Perez, P., Andrades, D. de, Polizeli, M. D. L. T. D. M., Rocha-Martin, J., & Fernandez-Lafuente, R. (2024). Reutilization of the most stable coimmobilized enzyme using glutaraldehyde chemistry to produce a new combi-biocatalyst when the coimmobilized enzyme with a lower stability is inactivated. ACS Sustainable Chemistry & Engineering, 12( 17), 6564-6572. doi:10.1021/acssuschemeng.3c08231 -
NLM
Carballares D, Abellanas-Perez P, Andrades D de, Polizeli MDLTDM, Rocha-Martin J, Fernandez-Lafuente R. Reutilization of the most stable coimmobilized enzyme using glutaraldehyde chemistry to produce a new combi-biocatalyst when the coimmobilized enzyme with a lower stability is inactivated [Internet]. ACS Sustainable Chemistry & Engineering. 2024 ; 12( 17): 6564-6572.[citado 2026 mar. 31 ] Available from: https://doi.org/10.1021/acssuschemeng.3c08231 -
Vancouver
Carballares D, Abellanas-Perez P, Andrades D de, Polizeli MDLTDM, Rocha-Martin J, Fernandez-Lafuente R. Reutilization of the most stable coimmobilized enzyme using glutaraldehyde chemistry to produce a new combi-biocatalyst when the coimmobilized enzyme with a lower stability is inactivated [Internet]. ACS Sustainable Chemistry & Engineering. 2024 ; 12( 17): 6564-6572.[citado 2026 mar. 31 ] Available from: https://doi.org/10.1021/acssuschemeng.3c08231 - Tuning almond lipase features by the buffer used during immobilization: the apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized
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