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  • Source: Process Biochemistry. Unidades: ICB, FCF

    Subjects: PLASMODIUM, MALÁRIA, VACINAS, ARMAZENAGEM DE MEDICAMENTOS

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      NOVAIS, Janaína Tenório et al. Evaluating the storage stability of a Plasmodium vivax circumsporozoite protein vaccine candidate. Process Biochemistry, v. 151, p. 126-136, 2025Tradução . . Disponível em: https://dx.doi.org/10.1016/j.procbio.2025.02.003. Acesso em: 08 out. 2025.
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      Novais, J. T., Marques, R. F., Gimenez, A. M., & Soares, I. da S. (2025). Evaluating the storage stability of a Plasmodium vivax circumsporozoite protein vaccine candidate. Process Biochemistry, 151, 126-136. doi:10.1016/j.procbio.2025.02.003
    • NLM

      Novais JT, Marques RF, Gimenez AM, Soares I da S. Evaluating the storage stability of a Plasmodium vivax circumsporozoite protein vaccine candidate [Internet]. Process Biochemistry. 2025 ; 151 126-136.[citado 2025 out. 08 ] Available from: https://dx.doi.org/10.1016/j.procbio.2025.02.003
    • Vancouver

      Novais JT, Marques RF, Gimenez AM, Soares I da S. Evaluating the storage stability of a Plasmodium vivax circumsporozoite protein vaccine candidate [Internet]. Process Biochemistry. 2025 ; 151 126-136.[citado 2025 out. 08 ] Available from: https://dx.doi.org/10.1016/j.procbio.2025.02.003
  • Source: Process Biochemistry. Unidades: FCF, EEL

    Subjects: CORANTES, BIOSSEGURANÇA

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      LINO, Nayara Kristina Borsato et al. Designing salt-induced polymer-polymer biphasic systems for optimized extraction of Monascus ruber biopigments obtained by fermentation of xylose-based medium. Process Biochemistry, v. 156, p. 8-19, 2025Tradução . . Disponível em: https://dx.doi.org/10.1016/j.procbio.2025.05.004. Acesso em: 08 out. 2025.
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      Lino, N. K. B., Arruda, G. L. de, Lourenço, F. R., Ebinuma, V. de C. S., Silva, S. S. da, Santos, J. C., & Lopes, A. M. (2025). Designing salt-induced polymer-polymer biphasic systems for optimized extraction of Monascus ruber biopigments obtained by fermentation of xylose-based medium. Process Biochemistry, 156, 8-19. doi:10.1016/j.procbio.2025.05.004
    • NLM

      Lino NKB, Arruda GL de, Lourenço FR, Ebinuma V de CS, Silva SS da, Santos JC, Lopes AM. Designing salt-induced polymer-polymer biphasic systems for optimized extraction of Monascus ruber biopigments obtained by fermentation of xylose-based medium [Internet]. Process Biochemistry. 2025 ; 156 8-19.[citado 2025 out. 08 ] Available from: https://dx.doi.org/10.1016/j.procbio.2025.05.004
    • Vancouver

      Lino NKB, Arruda GL de, Lourenço FR, Ebinuma V de CS, Silva SS da, Santos JC, Lopes AM. Designing salt-induced polymer-polymer biphasic systems for optimized extraction of Monascus ruber biopigments obtained by fermentation of xylose-based medium [Internet]. Process Biochemistry. 2025 ; 156 8-19.[citado 2025 out. 08 ] Available from: https://dx.doi.org/10.1016/j.procbio.2025.05.004
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BACTÉRIAS, ÁCIDO LÁCTICO, MICROBIOLOGIA DE ALIMENTOS

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      ZATER, Zohra Yasmine et al. Impact of a novel caseinolytic protease single mutation on Lactiplantibacillus pentosus growth performance. Process Biochemistry, v. 145, p. 145-152, 2024Tradução . . Disponível em: https://dx.doi.org/10.1016/j.procbio.2024.06.025. Acesso em: 08 out. 2025.
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      Zater, Z. Y., Merzoug, M., Baltaci, M. O., Todorov, S. D., Adiguzel, A., & Roudj, S. (2024). Impact of a novel caseinolytic protease single mutation on Lactiplantibacillus pentosus growth performance. Process Biochemistry, 145, 145-152. doi:10.1016/j.procbio.2024.06.025
    • NLM

      Zater ZY, Merzoug M, Baltaci MO, Todorov SD, Adiguzel A, Roudj S. Impact of a novel caseinolytic protease single mutation on Lactiplantibacillus pentosus growth performance [Internet]. Process Biochemistry. 2024 ; 145 145-152.[citado 2025 out. 08 ] Available from: https://dx.doi.org/10.1016/j.procbio.2024.06.025
    • Vancouver

      Zater ZY, Merzoug M, Baltaci MO, Todorov SD, Adiguzel A, Roudj S. Impact of a novel caseinolytic protease single mutation on Lactiplantibacillus pentosus growth performance [Internet]. Process Biochemistry. 2024 ; 145 145-152.[citado 2025 out. 08 ] Available from: https://dx.doi.org/10.1016/j.procbio.2024.06.025
  • Source: Process Biochemistry. Unidades: EP, Interunidades em 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: 08 out. 2025.
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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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2022.11.021
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: LEVEDURAS, ECOSSISTEMAS ANTÁRTICO

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      MOGUEL, Ignacio Sánchez et al. Antarctic yeasts as a source of L-asparaginase: characterization of a glutaminase-activity free Lasparaginase from psychrotolerant yeast Leucosporidium scottii L115. Process Biochemistry, v. 129, p. 121-132, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2023.03.003. Acesso em: 08 out. 2025.
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      Moguel, I. S., Silva, T. A. da C. e, Pullo, O. S. P., Santos, J. C. F., Freire, R. K. B., Carretero, G. P. B., et al. (2023). Antarctic yeasts as a source of L-asparaginase: characterization of a glutaminase-activity free Lasparaginase from psychrotolerant yeast Leucosporidium scottii L115. Process Biochemistry, 129, 121-132. doi:10.1016/j.procbio.2023.03.003
    • NLM

      Moguel IS, Silva TA da C e, Pullo OSP, Santos JCF, Freire RKB, Carretero GPB, Bueno J da L, Camacho Córdova DI, Santos JHPM, Sette LD, Pessoa Junior A. Antarctic yeasts as a source of L-asparaginase: characterization of a glutaminase-activity free Lasparaginase from psychrotolerant yeast Leucosporidium scottii L115 [Internet]. Process Biochemistry. 2023 ; 129 121-132.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2023.03.003
    • Vancouver

      Moguel IS, Silva TA da C e, Pullo OSP, Santos JCF, Freire RKB, Carretero GPB, Bueno J da L, Camacho Córdova DI, Santos JHPM, Sette LD, Pessoa Junior A. Antarctic yeasts as a source of L-asparaginase: characterization of a glutaminase-activity free Lasparaginase from psychrotolerant yeast Leucosporidium scottii L115 [Internet]. Process Biochemistry. 2023 ; 129 121-132.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2023.03.003
  • 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: 08 out. 2025.
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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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2023.02.023
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: LEUCEMIA, HIDRÓLISE

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      SOUSA, Lucas Silva de et al. A quaternary amine cryogel column for chromatographic capture of L-asparaginase. Process Biochemistry, v. 127, p. 92-98, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2023.01.016. Acesso em: 08 out. 2025.
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      Sousa, L. S. de, Chaves, F. da S., Ferraro, R. B., Pessoa Junior, A., & Minim, L. A. (2023). A quaternary amine cryogel column for chromatographic capture of L-asparaginase. Process Biochemistry, 127, 92-98. doi:10.1016/j.procbio.2023.01.016
    • NLM

      Sousa LS de, Chaves F da S, Ferraro RB, Pessoa Junior A, Minim LA. A quaternary amine cryogel column for chromatographic capture of L-asparaginase [Internet]. Process Biochemistry. 2023 ; 127 92-98.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2023.01.016
    • Vancouver

      Sousa LS de, Chaves F da S, Ferraro RB, Pessoa Junior A, Minim LA. A quaternary amine cryogel column for chromatographic capture of L-asparaginase [Internet]. Process Biochemistry. 2023 ; 127 92-98.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2023.01.016
  • 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: 08 out. 2025.
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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
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      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 2025 out. 08 ] 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 2025 out. 08 ] 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: 08 out. 2025.
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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
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      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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2020.11.005
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: PENICILLIUM, CULTURA DE CÉLULAS

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      VIEIRA, William Fernando et al. A novel multiple reactor system for the long-term production of L-asparaginase by Penicillium sp. LAMAI 505. Process Biochemistry, v. 90, p. 23-31, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2019.11.012. Acesso em: 08 out. 2025.
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      Vieira, W. F., Correa, H. T., Campos, E. S., Sette, L. D., Pessoa Junior, A., Cardoso, V. L., & Coutinho Filho, U. (2020). A novel multiple reactor system for the long-term production of L-asparaginase by Penicillium sp. LAMAI 505. Process Biochemistry, 90, 23-31. doi:10.1016/j.procbio.2019.11.012
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      Vieira WF, Correa HT, Campos ES, Sette LD, Pessoa Junior A, Cardoso VL, Coutinho Filho U. A novel multiple reactor system for the long-term production of L-asparaginase by Penicillium sp. LAMAI 505 [Internet]. Process Biochemistry. 2020 ; 90 23-31.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2019.11.012
    • Vancouver

      Vieira WF, Correa HT, Campos ES, Sette LD, Pessoa Junior A, Cardoso VL, Coutinho Filho U. A novel multiple reactor system for the long-term production of L-asparaginase by Penicillium sp. LAMAI 505 [Internet]. Process Biochemistry. 2020 ; 90 23-31.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2019.11.012
  • 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: 08 out. 2025.
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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
    • NLM

      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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2020.09.004
  • Source: Process Biochemistry. Unidade: EP

    Subjects: FOSFATOS, CLOSTRIDIUM, TOLERÂNCIA

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      ALVES, Rafael Ferraz et al. Enhancing acetic acid and 5-hydroxymethyl furfural tolerance of C. saccharoperbutylacetonicum through adaptive laboratory evolution. Process Biochemistry, v. 101, p. 179-189, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2020.11.013. Acesso em: 08 out. 2025.
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      Alves, R. F., Zetty-Arenas, A. M., Demirci, H., Dias, O., Rocha, I., Basso, T. O., & Freitas, S. (2020). Enhancing acetic acid and 5-hydroxymethyl furfural tolerance of C. saccharoperbutylacetonicum through adaptive laboratory evolution. Process Biochemistry, 101, 179-189. doi:10.1016/j.procbio.2020.11.013
    • NLM

      Alves RF, Zetty-Arenas AM, Demirci H, Dias O, Rocha I, Basso TO, Freitas S. Enhancing acetic acid and 5-hydroxymethyl furfural tolerance of C. saccharoperbutylacetonicum through adaptive laboratory evolution [Internet]. Process Biochemistry. 2020 ;101 179-189.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2020.11.013
    • Vancouver

      Alves RF, Zetty-Arenas AM, Demirci H, Dias O, Rocha I, Basso TO, Freitas S. Enhancing acetic acid and 5-hydroxymethyl furfural tolerance of C. saccharoperbutylacetonicum through adaptive laboratory evolution [Internet]. Process Biochemistry. 2020 ;101 179-189.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2020.11.013
  • 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: 08 out. 2025.
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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 2025 out. 08 ] 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 2025 out. 08 ] 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: 08 out. 2025.
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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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2019.03.009
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: LACTOBACILLUS, BACTÉRIAS LÁTICAS

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      SABO, Sabrina da Silva et al. Bacteriocin partitioning from a clarified fermentation broth of Lactobacillus plantarum ST16Pa in aqueous two-phase systems with sodium sulfate and choline-based salts as additives. Process Biochemistry, v. 66, p. 212-221, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2017.11.018. Acesso em: 08 out. 2025.
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      Sabo, S. da S., Lopes, A. M., Ebinuma, V. de C. S., Rangel-Yagui, C. de O., & Oliveira, R. P. de S. (2018). Bacteriocin partitioning from a clarified fermentation broth of Lactobacillus plantarum ST16Pa in aqueous two-phase systems with sodium sulfate and choline-based salts as additives. Process Biochemistry, 66, 212-221. doi:10.1016/j.procbio.2017.11.018
    • NLM

      Sabo S da S, Lopes AM, Ebinuma V de CS, Rangel-Yagui C de O, Oliveira RP de S. Bacteriocin partitioning from a clarified fermentation broth of Lactobacillus plantarum ST16Pa in aqueous two-phase systems with sodium sulfate and choline-based salts as additives [Internet]. Process Biochemistry. 2018 ; 66 212-221.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2017.11.018
    • Vancouver

      Sabo S da S, Lopes AM, Ebinuma V de CS, Rangel-Yagui C de O, Oliveira RP de S. Bacteriocin partitioning from a clarified fermentation broth of Lactobacillus plantarum ST16Pa in aqueous two-phase systems with sodium sulfate and choline-based salts as additives [Internet]. Process Biochemistry. 2018 ; 66 212-221.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2017.11.018
  • 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: 08 out. 2025.
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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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2017.05.017
  • Source: Process Biochemistry. Unidades: IF, IFSC

    Subjects: AEDES, SEMENTES, INSETICIDAS BIOLÓGICOS, CONTROLE DE INSETOS

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      DIAS, Lucas P. et al. A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activity against Aedes aegypti. Process Biochemistry, v. 57, p. 228-238, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2017.03.015. Acesso em: 08 out. 2025.
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      Dias, L. P., Oliveira, J. T. A., Rocha-Bezerra, L. C. B., Sousa, D. O. B., Costa, H. P. S., Araujo, N. M. S., et al. (2017). A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activity against Aedes aegypti. Process Biochemistry, 57, 228-238. doi:10.1016/j.procbio.2017.03.015
    • NLM

      Dias LP, Oliveira JTA, Rocha-Bezerra LCB, Sousa DOB, Costa HPS, Araujo NMS, Carvalho AFU, Tabosa PMS, Monteiro-Moreira ACO, Lobo MDP, Moreno FBMB, Rocha BAM, Lopes JL de S, Beltramini LM, Vasconcelos IM. A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activity against Aedes aegypti [Internet]. Process Biochemistry. 2017 ; 57 228-238.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2017.03.015
    • Vancouver

      Dias LP, Oliveira JTA, Rocha-Bezerra LCB, Sousa DOB, Costa HPS, Araujo NMS, Carvalho AFU, Tabosa PMS, Monteiro-Moreira ACO, Lobo MDP, Moreno FBMB, Rocha BAM, Lopes JL de S, Beltramini LM, Vasconcelos IM. A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activity against Aedes aegypti [Internet]. Process Biochemistry. 2017 ; 57 228-238.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2017.03.015
  • 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: 08 out. 2025.
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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 2025 out. 08 ] 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 2025 out. 08 ] 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: 08 out. 2025.
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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
    • NLM

      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 2025 out. 08 ] 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 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2016.01.004
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: ENZIMAS HIDROLÍTICAS, ALGAS MARINHAS, POLISSACARÍDEOS

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      GURPILHARES, Daniela de Borba et al. Algae’s sulfated polysaccharides modifications: potential use of microbial enzymes. Process Biochemistry, v. 51, n. 8, p. 989-998, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2016.04.020. Acesso em: 08 out. 2025.
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      Gurpilhares, D. de B., Moreira, T. R., Bueno, J. da L., Cinelli, L. P., Mazzola, P. G., Pessoa Junior, A., & Sette, L. D. (2016). Algae’s sulfated polysaccharides modifications: potential use of microbial enzymes. Process Biochemistry, 51( 8), 989-998. doi:10.1016/j.procbio.2016.04.020
    • NLM

      Gurpilhares D de B, Moreira TR, Bueno J da L, Cinelli LP, Mazzola PG, Pessoa Junior A, Sette LD. Algae’s sulfated polysaccharides modifications: potential use of microbial enzymes [Internet]. Process Biochemistry. 2016 ; 51( 8): 989-998.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2016.04.020
    • Vancouver

      Gurpilhares D de B, Moreira TR, Bueno J da L, Cinelli LP, Mazzola PG, Pessoa Junior A, Sette LD. Algae’s sulfated polysaccharides modifications: potential use of microbial enzymes [Internet]. Process Biochemistry. 2016 ; 51( 8): 989-998.[citado 2025 out. 08 ] Available from: https://doi.org/10.1016/j.procbio.2016.04.020

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