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  • Fonte: Discrete and Continuous Dynamical Systems, Series S. Unidade: ICMC

    Assuntos: TEORIA QUALITATIVA, SISTEMAS DINÂMICOS, GEOMETRIA ALGÉBRICA

    Versão AceitaAcesso à fonteDOIComo citar
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    • ABNT

      GARCÍA, Isaac A et al. A new characterization of the Jacobian conjecture in the real plane and some consequences. Discrete and Continuous Dynamical Systems, Series S, v. 18, n. 8, p. 2201-2210, 2025Tradução . . Disponível em: https://doi.org/10.3934/dcdss.2024201. Acesso em: 08 out. 2025.
    • APA

      García, I. A., Giné, J., Rodero, A. L., & Xiao, Y. (2025). A new characterization of the Jacobian conjecture in the real plane and some consequences. Discrete and Continuous Dynamical Systems, Series S, 18( 8), 2201-2210. doi:10.3934/dcdss.2024201
    • NLM

      García IA, Giné J, Rodero AL, Xiao Y. A new characterization of the Jacobian conjecture in the real plane and some consequences [Internet]. Discrete and Continuous Dynamical Systems, Series S. 2025 ; 18( 8): 2201-2210.[citado 2025 out. 08 ] Available from: https://doi.org/10.3934/dcdss.2024201
    • Vancouver

      García IA, Giné J, Rodero AL, Xiao Y. A new characterization of the Jacobian conjecture in the real plane and some consequences [Internet]. Discrete and Continuous Dynamical Systems, Series S. 2025 ; 18( 8): 2201-2210.[citado 2025 out. 08 ] Available from: https://doi.org/10.3934/dcdss.2024201
  • Fonte: Journal of Biotechnology. Unidade: FFCLRP

    Assuntos: ATIVAÇÃO ENZIMÁTICA, ENZIMAS, LIPASE, CATALISADORES

    Versão PublicadaAcesso à fonteDOIComo citar
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    • ABNT

      CHERNI, Oumaima et al. 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. Journal of Biotechnology, v. 391, p. 72-80, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jbiotec.2024.06.009. Acesso em: 08 out. 2025.
    • APA

      Cherni, O., Carballares, D., Siar, E. H., Abellanas-Perez, P., Andrades, D. de, Polizeli, M. D. L. T. D. M., et al. (2024). 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. Journal of Biotechnology, 391, 72-80. doi:10.1016/j.jbiotec.2024.06.009
    • NLM

      Cherni O, Carballares D, Siar EH, Abellanas-Perez P, Andrades D de, Polizeli MDLTDM, Rocha-Martin J, Bahri S, Fernandez-Lafuente R. 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 [Internet]. Journal of Biotechnology. 2024 ; 391 72-80.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.jbiotec.2024.06.009
    • Vancouver

      Cherni O, Carballares D, Siar EH, Abellanas-Perez P, Andrades D de, Polizeli MDLTDM, Rocha-Martin J, Bahri S, Fernandez-Lafuente R. 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 [Internet]. Journal of Biotechnology. 2024 ; 391 72-80.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.jbiotec.2024.06.009
  • Fonte: ACS Sustainable Chemistry & Engineering. Unidade: FFCLRP

    Assuntos: ENZIMAS, CATALISADORES, DESINFETANTES, REAÇÕES QUÍMICAS

    Versão PublicadaAcesso à fonteDOIComo citar
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    • 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: 08 out. 2025.
    • 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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1021/acssuschemeng.3c08231

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