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  • Source: Process Biochemistry. Unidades: EP, BIOTECNOLOGIA, EACH

    Subjects: VACINA ANTIRRÁBICA, VÍRUS DA RAIVA, BIOTECNOLOGIA, BIOPROCESSOS, RAIVA

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      GUARDALINI, Luis Giovani Oliveira et al. Oxygen uptake and transfer rates throughout production of recombinant baculovirus and rabies virus-like particles. Process Biochemistry, v. 124, n. Ja 2023, p. 189-200, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2022.11.021. Acesso em: 02 nov. 2024.
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      Guardalini, L. G. O., Cavalcante, P. E. da S., Leme, J., Mello, R. G. de, Bernardino, T. C., Astray, R. M., et al. (2023). Oxygen uptake and transfer rates throughout production of recombinant baculovirus and rabies virus-like particles. Process Biochemistry, 124( Ja 2023), 189-200. doi:10.1016/j.procbio.2022.11.021
    • NLM

      Guardalini LGO, Cavalcante PE da S, Leme J, Mello RG de, Bernardino TC, Astray RM, Tonso A, Jorge SAC, Fernández Núñez EG. Oxygen uptake and transfer rates throughout production of recombinant baculovirus and rabies virus-like particles [Internet]. Process Biochemistry. 2023 ; 124( Ja 2023): 189-200.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2022.11.021
    • Vancouver

      Guardalini LGO, Cavalcante PE da S, Leme J, Mello RG de, Bernardino TC, Astray RM, Tonso A, Jorge SAC, Fernández Núñez EG. Oxygen uptake and transfer rates throughout production of recombinant baculovirus and rabies virus-like particles [Internet]. Process Biochemistry. 2023 ; 124( Ja 2023): 189-200.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2022.11.021
  • Source: Process Biochemistry. Unidades: EACH, FCF

    Assunto: QUITOSANA

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      CERÓN, Annie A. et al. Study of stability, kinetic parameters and release of lysozyme immobilized on chitosan microspheres by crosslinking and covalent attachment for cotton fabric functionalization. Process Biochemistry, v. 128, p. 116-125, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2023.02.023. Acesso em: 02 nov. 2024.
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      Cerón, A. A., Costa, S. A. da, Imbernon, R. A. L., Queiroz, R. de, Castro, J. de, Ferraz, H. G., et al. (2023). Study of stability, kinetic parameters and release of lysozyme immobilized on chitosan microspheres by crosslinking and covalent attachment for cotton fabric functionalization. Process Biochemistry, 128, 116-125. doi:10.1016/j.procbio.2023.02.023
    • NLM

      Cerón AA, Costa SA da, Imbernon RAL, Queiroz R de, Castro J de, Ferraz HG, Oliveira R, Costa SM da. Study of stability, kinetic parameters and release of lysozyme immobilized on chitosan microspheres by crosslinking and covalent attachment for cotton fabric functionalization [Internet]. Process Biochemistry. 2023 ; 128 116-125.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2023.02.023
    • Vancouver

      Cerón AA, Costa SA da, Imbernon RAL, Queiroz R de, Castro J de, Ferraz HG, Oliveira R, Costa SM da. Study of stability, kinetic parameters and release of lysozyme immobilized on chitosan microspheres by crosslinking and covalent attachment for cotton fabric functionalization [Internet]. Process Biochemistry. 2023 ; 128 116-125.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2023.02.023
  • Source: Process Biochemistry. Unidades: FCF, EP

    Subjects: LEUCEMIA, PROTEÍNAS

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      KLEINGESINDS, Eduardo Krebs et al. Downstream process and evaluation of the concomitant impact of a recombinant glycosylated L-asparaginase on leukemic cancer cells and the bone marrow tumor microenvironment. Process Biochemistry, v. 131, p. 41–51, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2023.06.006. Acesso em: 02 nov. 2024.
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      Kleingesinds, E. K., Parizotto, L. de A., Effer, B., Monteiro, G., Long, P. F., Berdugo, Y. A., et al. (2023). Downstream process and evaluation of the concomitant impact of a recombinant glycosylated L-asparaginase on leukemic cancer cells and the bone marrow tumor microenvironment. Process Biochemistry, 131, 41–51. doi:10.1016/j.procbio.2023.06.006
    • NLM

      Kleingesinds EK, Parizotto L de A, Effer B, Monteiro G, Long PF, Berdugo YA, Behrends V, Esposito MT, Calle Y, Pessoa Junior A. Downstream process and evaluation of the concomitant impact of a recombinant glycosylated L-asparaginase on leukemic cancer cells and the bone marrow tumor microenvironment [Internet]. Process Biochemistry. 2023 ; 131 41–51.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2023.06.006
    • Vancouver

      Kleingesinds EK, Parizotto L de A, Effer B, Monteiro G, Long PF, Berdugo YA, Behrends V, Esposito MT, Calle Y, Pessoa Junior A. Downstream process and evaluation of the concomitant impact of a recombinant glycosylated L-asparaginase on leukemic cancer cells and the bone marrow tumor microenvironment [Internet]. Process Biochemistry. 2023 ; 131 41–51.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2023.06.006
  • Source: Process Biochemistry. Unidades: IQSC, EESC

    Subjects: TRANSPORTE DE MASSA, DIÓXIDO DE CARBONO, COMPOSTOS ORGÂNICOS

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      ROJAS, Melida Del Pilar Anzola et al. Enhancing the gas–liquid mass transfer during microbial electrosynthesis by the variation of CO2 flow rate. Process Biochemistry, v. 101, p. 50-58, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2020.11.005. Acesso em: 02 nov. 2024.
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      Rojas, M. D. P. A., Zaiat, M., Gonzalez, E. R., Wever, H. D., & Pant, D. (2021). Enhancing the gas–liquid mass transfer during microbial electrosynthesis by the variation of CO2 flow rate. Process Biochemistry, 101, 50-58. doi:10.1016/j.procbio.2020.11.005
    • NLM

      Rojas MDPA, Zaiat M, Gonzalez ER, Wever HD, Pant D. Enhancing the gas–liquid mass transfer during microbial electrosynthesis by the variation of CO2 flow rate [Internet]. Process Biochemistry. 2021 ; 101 50-58.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2020.11.005
    • Vancouver

      Rojas MDPA, Zaiat M, Gonzalez ER, Wever HD, Pant D. Enhancing the gas–liquid mass transfer during microbial electrosynthesis by the variation of CO2 flow rate [Internet]. Process Biochemistry. 2021 ; 101 50-58.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2020.11.005
  • Source: Process Biochemistry. Unidades: FMRP, FFCLRP, FCFRP

    Subjects: BIOQUÍMICA, GLICOSE, BIOMASSA, ENZIMAS, CELULOSE, BIOPROCESSOS

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      ALMEIDA, Paula Zaghetto de et al. Heterologous production and biochemical characterization of a new highly glucose tolerant GH1 β-glucosidase from Anoxybacillus thermarum. Process Biochemistry, v. 99, p. 1-8, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2020.08.013. Acesso em: 02 nov. 2024.
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      Almeida, P. Z. de, Oliveira, T. B. de, Lucas, R. C. de, Salgado, J. C. dos S., Pérez, M. M., Gálan, B., et al. (2020). Heterologous production and biochemical characterization of a new highly glucose tolerant GH1 β-glucosidase from Anoxybacillus thermarum. Process Biochemistry, 99, 1-8. doi:10.1016/j.procbio.2020.08.013
    • NLM

      Almeida PZ de, Oliveira TB de, Lucas RC de, Salgado JC dos S, Pérez MM, Gálan B, García JL, Polizeli M de LT de M. Heterologous production and biochemical characterization of a new highly glucose tolerant GH1 β-glucosidase from Anoxybacillus thermarum [Internet]. Process Biochemistry. 2020 ; 99 1-8.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2020.08.013
    • Vancouver

      Almeida PZ de, Oliveira TB de, Lucas RC de, Salgado JC dos S, Pérez MM, Gálan B, García JL, Polizeli M de LT de M. Heterologous production and biochemical characterization of a new highly glucose tolerant GH1 β-glucosidase from Anoxybacillus thermarum [Internet]. Process Biochemistry. 2020 ; 99 1-8.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2020.08.013
  • Source: Process Biochemistry. Unidade: IQSC

    Subjects: BIOQUÍMICA, CICLINAS, PROTEÍNAS

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      COELHO, Fernanda et al. Overexpression and refolding of human Cyclin D3.: A reliable method or not?. Process Biochemistry, v. 90, p. 196–201 September 2020, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2020.09.004. Acesso em: 02 nov. 2024.
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      Coelho, F., Pepino, R. de O., Alencar, D. P., Santos, J. L., & Canduri, F. (2020). Overexpression and refolding of human Cyclin D3.: A reliable method or not? Process Biochemistry, 90, 196–201 September 2020. doi:10.1016/j.procbio.2020.09.004
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      Coelho F, Pepino R de O, Alencar DP, Santos JL, Canduri F. Overexpression and refolding of human Cyclin D3.: A reliable method or not? [Internet]. Process Biochemistry. 2020 ; 90 196–201 September 2020.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2020.09.004
    • Vancouver

      Coelho F, Pepino R de O, Alencar DP, Santos JL, Canduri F. Overexpression and refolding of human Cyclin D3.: A reliable method or not? [Internet]. Process Biochemistry. 2020 ; 90 196–201 September 2020.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2020.09.004
  • Source: Process Biochemistry. Unidade: IFSC

    Subjects: ENZIMAS, BIOCOMBUSTÍVEIS, ETANOL

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      HANS, Meenu et al. A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation. Process Biochemistry, v. 85, p. 125-134, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2019.06.019. Acesso em: 02 nov. 2024.
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      Hans, M., Kumar, S., Chandel, A. K., & Polikarpov, I. (2019). A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation. Process Biochemistry, 85, 125-134. doi:10.1016/j.procbio.2019.06.019
    • NLM

      Hans M, Kumar S, Chandel AK, Polikarpov I. A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation [Internet]. Process Biochemistry. 2019 ; 85 125-134.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2019.06.019
    • Vancouver

      Hans M, Kumar S, Chandel AK, Polikarpov I. A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation [Internet]. Process Biochemistry. 2019 ; 85 125-134.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2019.06.019
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BIOFARMÁCIA, ENZIMAS, PROTEÍNAS

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      WLODARCZYK, Samarina Rodrigues et al. Effect of osmolytes on the activity of anti-cancer enzyme L-Asparaginase II from Erwinia chrysanthemi. Process Biochemistry, v. 81, p. 123-131, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2019.03.009. Acesso em: 02 nov. 2024.
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      Wlodarczyk, S. R., Silva, T. A. C., Pessoa Junior, A., Madeira, P., & Monteiro, G. (2019). Effect of osmolytes on the activity of anti-cancer enzyme L-Asparaginase II from Erwinia chrysanthemi. Process Biochemistry, 81, 123-131. doi:10.1016/j.procbio.2019.03.009
    • NLM

      Wlodarczyk SR, Silva TAC, Pessoa Junior A, Madeira P, Monteiro G. Effect of osmolytes on the activity of anti-cancer enzyme L-Asparaginase II from Erwinia chrysanthemi [Internet]. Process Biochemistry. 2019 ; 81 123-131.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2019.03.009
    • Vancouver

      Wlodarczyk SR, Silva TAC, Pessoa Junior A, Madeira P, Monteiro G. Effect of osmolytes on the activity of anti-cancer enzyme L-Asparaginase II from Erwinia chrysanthemi [Internet]. Process Biochemistry. 2019 ; 81 123-131.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2019.03.009
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: CAMU-CAMU, ANTIOXIDANTES

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      FUJITA, Alice et al. Improving anti-hyperglycemic and anti-hypertensive properties of camucamu (Myriciaria dubia Mc. Vaugh) using lactic acid bacterial fermentation. Process Biochemistry, v. 59, p. 133-140, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2017.05.017. Acesso em: 02 nov. 2024.
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      Fujita, A., Sarkar, D., Genovese, M. I., & Shetty, K. (2017). Improving anti-hyperglycemic and anti-hypertensive properties of camucamu (Myriciaria dubia Mc. Vaugh) using lactic acid bacterial fermentation. Process Biochemistry, 59, 133-140. doi:10.1016/j.procbio.2017.05.017
    • NLM

      Fujita A, Sarkar D, Genovese MI, Shetty K. Improving anti-hyperglycemic and anti-hypertensive properties of camucamu (Myriciaria dubia Mc. Vaugh) using lactic acid bacterial fermentation [Internet]. Process Biochemistry. 2017 ; 59 133-140.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2017.05.017
    • Vancouver

      Fujita A, Sarkar D, Genovese MI, Shetty K. Improving anti-hyperglycemic and anti-hypertensive properties of camucamu (Myriciaria dubia Mc. Vaugh) using lactic acid bacterial fermentation [Internet]. Process Biochemistry. 2017 ; 59 133-140.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2017.05.017
  • Source: Process Biochemistry. Unidade: EESC

    Subjects: OXIGÊNIO, NITROGÊNIO, NITRIFICAÇÃO, DESNITRIFICAÇÃO, AMÔNIA, OXIDAÇÃO

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      ZHIXUAN, Yin et al. Importance of the combined effects of dissolved oxygen and pH on optimization of nitrogen removal in anammox-enriched granular sludge. Process Biochemistry, v. 51, n. 9, p. 1274-1282, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2016.05.025. Acesso em: 02 nov. 2024.
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      Zhixuan, Y., Santos, C. E. D. dos, Gonzalez Vilaplana, J., Sobotka, D., Czerwionka, K., Damianovic, M. H. R. Z., et al. (2016). Importance of the combined effects of dissolved oxygen and pH on optimization of nitrogen removal in anammox-enriched granular sludge. Process Biochemistry, 51( 9), 1274-1282. doi:10.1016/j.procbio.2016.05.025
    • NLM

      Zhixuan Y, Santos CED dos, Gonzalez Vilaplana J, Sobotka D, Czerwionka K, Damianovic MHRZ, Li X, Fernández Morales FJ, Makinia J. Importance of the combined effects of dissolved oxygen and pH on optimization of nitrogen removal in anammox-enriched granular sludge [Internet]. Process Biochemistry. 2016 ; 51( 9): 1274-1282.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2016.05.025
    • Vancouver

      Zhixuan Y, Santos CED dos, Gonzalez Vilaplana J, Sobotka D, Czerwionka K, Damianovic MHRZ, Li X, Fernández Morales FJ, Makinia J. Importance of the combined effects of dissolved oxygen and pH on optimization of nitrogen removal in anammox-enriched granular sludge [Internet]. Process Biochemistry. 2016 ; 51( 9): 1274-1282.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2016.05.025
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: LÍQUIDOS IÔNICOS, SURFACTANTES, ABACAXI

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      VICENTE, Filipa A et al. Recovery of bromelain from pineapple stem residues using aqueous micellar two-phase systems with ionic liquids as co-surfactants. Process Biochemistry, v. 51, p. 528-534, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2016.01.004. Acesso em: 02 nov. 2024.
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      Vicente, F. A., Lario, L. D., Pessoa Junior, A., & Ventura, S. P. M. (2016). Recovery of bromelain from pineapple stem residues using aqueous micellar two-phase systems with ionic liquids as co-surfactants. Process Biochemistry, 51, 528-534. doi:10.1016/j.procbio.2016.01.004
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      Vicente FA, Lario LD, Pessoa Junior A, Ventura SPM. Recovery of bromelain from pineapple stem residues using aqueous micellar two-phase systems with ionic liquids as co-surfactants [Internet]. Process Biochemistry. 2016 ; 51 528-534.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2016.01.004
    • Vancouver

      Vicente FA, Lario LD, Pessoa Junior A, Ventura SPM. Recovery of bromelain from pineapple stem residues using aqueous micellar two-phase systems with ionic liquids as co-surfactants [Internet]. Process Biochemistry. 2016 ; 51 528-534.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2016.01.004
  • Source: Process Biochemistry. Unidade: FFCLRP

    Subjects: HYPOCREALES, LIPASE (ISOLAMENTO E PURIFICAÇÃO), SOLVENTE, BIOTECNOLOGIA

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      PEREIRA, Marita Gimenez et al. Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: determination of thermal and organic solvent stabilities for applications in the oleochemical industry. Process Biochemistry, v. 50, n. 4, p. 561–570, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2014.12.027. Acesso em: 02 nov. 2024.
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      Pereira, M. G., Facchini, F. D. A., Filó, L. E. C., Polizeli, A. M., Vici, A. C., Jorge, J. A., et al. (2015). Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: determination of thermal and organic solvent stabilities for applications in the oleochemical industry. Process Biochemistry, 50( 4), 561–570. doi:10.1016/j.procbio.2014.12.027
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      Pereira MG, Facchini FDA, Filó LEC, Polizeli AM, Vici AC, Jorge JA, Lorente GF, Pessela BC, Guisan JM, Polizeli M de LT de M. Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: determination of thermal and organic solvent stabilities for applications in the oleochemical industry [Internet]. Process Biochemistry. 2015 ; 50( 4): 561–570.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2014.12.027
    • Vancouver

      Pereira MG, Facchini FDA, Filó LEC, Polizeli AM, Vici AC, Jorge JA, Lorente GF, Pessela BC, Guisan JM, Polizeli M de LT de M. Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: determination of thermal and organic solvent stabilities for applications in the oleochemical industry [Internet]. Process Biochemistry. 2015 ; 50( 4): 561–570.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2014.12.027
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: LÍQUIDOS IÔNICOS, ELETRÓLITOS, SÓDIO

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      SANTOS, João H. P. M et al. Ionic liquids as a novel class of electrolytes in polymeric aqueous biphasic systems. Process Biochemistry, v. 50, n. 4, p. 661-668, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2015.02.001. Acesso em: 02 nov. 2024.
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      Santos, J. H. P. M., Silva, F. A. e, Coutinho, J. A. P., Ventura, S. P. M., & Pessoa Junior, A. (2015). Ionic liquids as a novel class of electrolytes in polymeric aqueous biphasic systems. Process Biochemistry, 50( 4), 661-668. doi:10.1016/j.procbio.2015.02.001
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      Santos JHPM, Silva FA e, Coutinho JAP, Ventura SPM, Pessoa Junior A. Ionic liquids as a novel class of electrolytes in polymeric aqueous biphasic systems [Internet]. Process Biochemistry. 2015 ; 50( 4): 661-668.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2015.02.001
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      Santos JHPM, Silva FA e, Coutinho JAP, Ventura SPM, Pessoa Junior A. Ionic liquids as a novel class of electrolytes in polymeric aqueous biphasic systems [Internet]. Process Biochemistry. 2015 ; 50( 4): 661-668.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2015.02.001
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: EXTRAÇÃO DE LÍQUIDOS, PENICILLIUM

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      BARROS, Kleber Vânio Gomes et al. PEG/NaPA aqueous two-phase systems for the purification of proteases expressed by Penicillium restrictum from Brazilian Savanna. Process Biochemistry, v. 49, n. 12, p. 2305-2312, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2014.09.022. Acesso em: 02 nov. 2024.
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      Barros, K. V. G., Souza, P. M., Freitas, M. M., Ferreira Filho, E. X., Pessoa Junior, A., & Magalhães, P. O. (2014). PEG/NaPA aqueous two-phase systems for the purification of proteases expressed by Penicillium restrictum from Brazilian Savanna. Process Biochemistry, 49( 12), 2305-2312. doi:10.1016/j.procbio.2014.09.022
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      Barros KVG, Souza PM, Freitas MM, Ferreira Filho EX, Pessoa Junior A, Magalhães PO. PEG/NaPA aqueous two-phase systems for the purification of proteases expressed by Penicillium restrictum from Brazilian Savanna [Internet]. Process Biochemistry. 2014 ; 49( 12): 2305-2312.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2014.09.022
    • Vancouver

      Barros KVG, Souza PM, Freitas MM, Ferreira Filho EX, Pessoa Junior A, Magalhães PO. PEG/NaPA aqueous two-phase systems for the purification of proteases expressed by Penicillium restrictum from Brazilian Savanna [Internet]. Process Biochemistry. 2014 ; 49( 12): 2305-2312.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2014.09.022
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: EXTRAÇÃO DE LÍQUIDOS, SOLUBILIZAÇÃO

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      LOPES, André Moreni et al. 5CN05 partitioning in an aqueous two-phase system: a new approach to the solubilization of hydrophobic drugs. Process Biochemistry, v. 49, n. 9, p. 1555-1561, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2014.05.017. Acesso em: 02 nov. 2024.
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      Lopes, A. M., Santos-Ebinuma, V. de C., Apolinário, A. C., Mendonça Junior, F. J. B., Damasceno, B. P. G. de L., Pessoa Junior, A., & Silva, J. A. da. (2014). 5CN05 partitioning in an aqueous two-phase system: a new approach to the solubilization of hydrophobic drugs. Process Biochemistry, 49( 9), 1555-1561. doi:10.1016/j.procbio.2014.05.017
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      Lopes AM, Santos-Ebinuma V de C, Apolinário AC, Mendonça Junior FJB, Damasceno BPG de L, Pessoa Junior A, Silva JA da. 5CN05 partitioning in an aqueous two-phase system: a new approach to the solubilization of hydrophobic drugs [Internet]. Process Biochemistry. 2014 ; 49( 9): 1555-1561.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2014.05.017
    • Vancouver

      Lopes AM, Santos-Ebinuma V de C, Apolinário AC, Mendonça Junior FJB, Damasceno BPG de L, Pessoa Junior A, Silva JA da. 5CN05 partitioning in an aqueous two-phase system: a new approach to the solubilization of hydrophobic drugs [Internet]. Process Biochemistry. 2014 ; 49( 9): 1555-1561.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2014.05.017
  • Source: Process Biochemistry. Unidade: FCFRP

    Subjects: ENZIMAS PROTEOLÍTICAS, EUPHORBIACEAE, ENZIMOLOGIA

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      MORO, L. P. et al. Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii. Process Biochemistry, v. 48, n. 4, p. 633-637, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2013.02.017. Acesso em: 02 nov. 2024.
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      Moro, L. P., Cabral, H., Okamoto, D. N., Hirata, I., Juliano, M. A., Juliano, L., & Bonilla-Rodriguez, G. O. (2013). Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii. Process Biochemistry, 48( 4), 633-637. doi:10.1016/j.procbio.2013.02.017
    • NLM

      Moro LP, Cabral H, Okamoto DN, Hirata I, Juliano MA, Juliano L, Bonilla-Rodriguez GO. Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii [Internet]. Process Biochemistry. 2013 ; 48( 4): 633-637.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2013.02.017
    • Vancouver

      Moro LP, Cabral H, Okamoto DN, Hirata I, Juliano MA, Juliano L, Bonilla-Rodriguez GO. Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii [Internet]. Process Biochemistry. 2013 ; 48( 4): 633-637.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2013.02.017
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: IMUNOGLOBULINAS, ANTICORPOS

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      MALPIEDI, Luciana Pellegrini et al. Single-chain antibody fragments: purification methodologies. Process Biochemistry, v. 48, n. 8, p. 1242-1251, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2013.06.008. Acesso em: 02 nov. 2024.
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      Malpiedi, L. P., Diaz, C. A., Nerli, B. B., & Pessoa Junior, A. (2013). Single-chain antibody fragments: purification methodologies. Process Biochemistry, 48( 8), 1242-1251. doi:10.1016/j.procbio.2013.06.008
    • NLM

      Malpiedi LP, Diaz CA, Nerli BB, Pessoa Junior A. Single-chain antibody fragments: purification methodologies [Internet]. Process Biochemistry. 2013 ; 48( 8): 1242-1251.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2013.06.008
    • Vancouver

      Malpiedi LP, Diaz CA, Nerli BB, Pessoa Junior A. Single-chain antibody fragments: purification methodologies [Internet]. Process Biochemistry. 2013 ; 48( 8): 1242-1251.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2013.06.008
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: FERMENTAÇÃO, EXTRAÇÃO DE LÍQUIDOS, STREPTOMYCES

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      PEREIRA, Jorge F. B et al. Extraction of tetracycline from fermentation broth using aqueous two-phase systems composed of polyethylene glycol and cholinium-based salts. Process Biochemistry, v. 48, n. 4, p. 716-722, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2013.02.025. Acesso em: 02 nov. 2024.
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      Pereira, J. F. B., Vicente, F., Santos-Ebinuma, V. de C., Araujo, J. M. de, Pessoa Junior, A., Freire, M. G., & Coutinho, J. A. P. (2013). Extraction of tetracycline from fermentation broth using aqueous two-phase systems composed of polyethylene glycol and cholinium-based salts. Process Biochemistry, 48( 4), 716-722. doi:10.1016/j.procbio.2013.02.025
    • NLM

      Pereira JFB, Vicente F, Santos-Ebinuma V de C, Araujo JM de, Pessoa Junior A, Freire MG, Coutinho JAP. Extraction of tetracycline from fermentation broth using aqueous two-phase systems composed of polyethylene glycol and cholinium-based salts [Internet]. Process Biochemistry. 2013 ; 48( 4): 716-722.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2013.02.025
    • Vancouver

      Pereira JFB, Vicente F, Santos-Ebinuma V de C, Araujo JM de, Pessoa Junior A, Freire MG, Coutinho JAP. Extraction of tetracycline from fermentation broth using aqueous two-phase systems composed of polyethylene glycol and cholinium-based salts [Internet]. Process Biochemistry. 2013 ; 48( 4): 716-722.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2013.02.025
  • Source: Process Biochemistry. Unidade: FFCLRP

    Subjects: ASPERGILLUS, EXPRESSÃO GÊNICA, ENZIMAS

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      DAMÁSIO, André Ricardo de Lima et al. Improvement of fungal arabinofuranosidase thermal stability by reversible immobilization. Process Biochemistry, v. 47, n. 12, p. 2411-2417, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2012.09.024. Acesso em: 02 nov. 2024.
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      Damásio, A. R. de L., Pessela, B. C., Segato, F., Prade, R. A., Guisan, J. M., & Polizeli, M. de L. T. de M. (2012). Improvement of fungal arabinofuranosidase thermal stability by reversible immobilization. Process Biochemistry, 47( 12), 2411-2417. doi:10.1016/j.procbio.2012.09.024
    • NLM

      Damásio AR de L, Pessela BC, Segato F, Prade RA, Guisan JM, Polizeli M de LT de M. Improvement of fungal arabinofuranosidase thermal stability by reversible immobilization [Internet]. Process Biochemistry. 2012 ; 47( 12): 2411-2417.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2012.09.024
    • Vancouver

      Damásio AR de L, Pessela BC, Segato F, Prade RA, Guisan JM, Polizeli M de LT de M. Improvement of fungal arabinofuranosidase thermal stability by reversible immobilization [Internet]. Process Biochemistry. 2012 ; 47( 12): 2411-2417.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2012.09.024
  • Source: Process Biochemistry. Unidade: ESALQ

    Subjects: INIBIDORES DE ENZIMAS, PROTEINASES, PLANTAS PRODUTORAS DE PESTICIDA, INSETICIDAS BIOLÓGICOS, CONTROLE BIOLÓGICO, BROCAS (INSETOS NOCIVOS)

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      SILVA, Walciane da et al. Evaluation of the Adenanthera pavonina seed proteinase inhibitor (ApTI) as a bioinsecticidal tool with potential for the control of Diatraea saccharalis. Process Biochemistry, v. 47, n. 2, p. 257\2013263, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2011.11.002. Acesso em: 02 nov. 2024.
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      Silva, W. da, Freire, M. das G. M., Parra, J. R. P., Marangoni, S., & Macedo, M. L. R. (2012). Evaluation of the Adenanthera pavonina seed proteinase inhibitor (ApTI) as a bioinsecticidal tool with potential for the control of Diatraea saccharalis. Process Biochemistry, 47( 2), 257\2013263. doi:10.1016/j.procbio.2011.11.002
    • NLM

      Silva W da, Freire M das GM, Parra JRP, Marangoni S, Macedo MLR. Evaluation of the Adenanthera pavonina seed proteinase inhibitor (ApTI) as a bioinsecticidal tool with potential for the control of Diatraea saccharalis [Internet]. Process Biochemistry. 2012 ; 47( 2): 257\2013263.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2011.11.002
    • Vancouver

      Silva W da, Freire M das GM, Parra JRP, Marangoni S, Macedo MLR. Evaluation of the Adenanthera pavonina seed proteinase inhibitor (ApTI) as a bioinsecticidal tool with potential for the control of Diatraea saccharalis [Internet]. Process Biochemistry. 2012 ; 47( 2): 257\2013263.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.procbio.2011.11.002

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