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  • 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: 30 set. 2024.
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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 2024 set. 30 ] 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 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2023.03.003
  • 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: 30 set. 2024.
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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 2024 set. 30 ] 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 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2023.01.016
  • 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: 30 set. 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 set. 30 ] 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 set. 30 ] 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: 30 set. 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 set. 30 ] 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 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2023.06.006
  • 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: 30 set. 2024.
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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
    • NLM

      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 2024 set. 30 ] 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 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2019.11.012
  • 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: 30 set. 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 set. 30 ] 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 set. 30 ] 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: 30 set. 2024.
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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 2024 set. 30 ] 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 2024 set. 30 ] 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: 30 set. 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 set. 30 ] 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 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2017.05.017
  • 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: 30 set. 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
    • 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 2024 set. 30 ] 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 set. 30 ] 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: 30 set. 2024.
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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 2024 set. 30 ] 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 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2016.04.020
  • 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: 30 set. 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
    • NLM

      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 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2015.02.001
    • Vancouver

      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 set. 30 ] 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: 30 set. 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
    • NLM

      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 set. 30 ] 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 set. 30 ] 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: 30 set. 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 set. 30 ] 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 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2014.05.017
  • 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: 30 set. 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
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      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 set. 30 ] 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 set. 30 ] 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: 30 set. 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 set. 30 ] 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 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2013.02.025
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: ADSORÇÃO, GOMAS E RESINAS, SACAROSE, BIOQUÍMICA INDUSTRIAL

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      TOMOTANI, Ester Junko e VITOLO, Michele. Catalytic performance of invertase immobilized by adsorption on anionic exchange resin. Process Biochemistry, v. 41, n. 6, p. 1325-1331, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2006.01.004. Acesso em: 30 set. 2024.
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      Tomotani, E. J., & Vitolo, M. (2006). Catalytic performance of invertase immobilized by adsorption on anionic exchange resin. Process Biochemistry, 41( 6), 1325-1331. doi:10.1016/j.procbio.2006.01.004
    • NLM

      Tomotani EJ, Vitolo M. Catalytic performance of invertase immobilized by adsorption on anionic exchange resin [Internet]. Process Biochemistry. 2006 ; 41( 6): 1325-1331.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2006.01.004
    • Vancouver

      Tomotani EJ, Vitolo M. Catalytic performance of invertase immobilized by adsorption on anionic exchange resin [Internet]. Process Biochemistry. 2006 ; 41( 6): 1325-1331.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2006.01.004
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BIOTECNOLOGIA, ENZIMAS, FERMENTAÇÃO (PROCESSOS)

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      GURPILHARES, Daniela de Borba e PESSOA JUNIOR, Adalberto e ROBERTO, Inês Conceição. Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design. Process Biochemistry, v. 41, n. 3, p. 631-637, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2005.08.008. Acesso em: 30 set. 2024.
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      Gurpilhares, D. de B., Pessoa Junior, A., & Roberto, I. C. (2006). Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design. Process Biochemistry, 41( 3), 631-637. doi:10.1016/j.procbio.2005.08.008
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      Gurpilhares D de B, Pessoa Junior A, Roberto IC. Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design [Internet]. Process Biochemistry. 2006 ; 41( 3): 631-637.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2005.08.008
    • Vancouver

      Gurpilhares D de B, Pessoa Junior A, Roberto IC. Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design [Internet]. Process Biochemistry. 2006 ; 41( 3): 631-637.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/j.procbio.2005.08.008
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BIOQUÍMICA, CANDIDA, FERMENTAÇÃO

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      SILVA, Silvio Silvério da et al. Use of a fluidized bed reactor operated in semi-continuous mode for xylose-to-xylitol conversion by Candida guilliermondii immobilized on porous glass. Process Biochemistry, v. 38, n. 6, p. 903-907, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0032-9592(02)00177-2. Acesso em: 30 set. 2024.
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      Silva, S. S. da, Santos, J. C., Carvalho, W., Aracava, K. K., & Vitolo, M. (2003). Use of a fluidized bed reactor operated in semi-continuous mode for xylose-to-xylitol conversion by Candida guilliermondii immobilized on porous glass. Process Biochemistry, 38( 6), 903-907. doi:10.1016/s0032-9592(02)00177-2
    • NLM

      Silva SS da, Santos JC, Carvalho W, Aracava KK, Vitolo M. Use of a fluidized bed reactor operated in semi-continuous mode for xylose-to-xylitol conversion by Candida guilliermondii immobilized on porous glass [Internet]. Process Biochemistry. 2003 ; 38( 6): 903-907.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/s0032-9592(02)00177-2
    • Vancouver

      Silva SS da, Santos JC, Carvalho W, Aracava KK, Vitolo M. Use of a fluidized bed reactor operated in semi-continuous mode for xylose-to-xylitol conversion by Candida guilliermondii immobilized on porous glass [Internet]. Process Biochemistry. 2003 ; 38( 6): 903-907.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/s0032-9592(02)00177-2
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BIOQUÍMICA, CANDIDA, CANA-DE-AÇÚCAR, BIOTECNOLOGIA

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      RODRIGUES, Rita de Cássia Lacerda Brambilla et al. Response surface methodology for xylitol production from sugarcane bagasse hemicellulosic hydrolyzate using controlled vacuum evaporation process variables. Process Biochemistry, v. 38, n. 8, p. 1231-1237, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0032-9592(02)00290-x. Acesso em: 30 set. 2024.
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      Rodrigues, R. de C. L. B., Felipe, M. das G. de A., Silva, J. B. de A. e, & Vitolo, M. (2003). Response surface methodology for xylitol production from sugarcane bagasse hemicellulosic hydrolyzate using controlled vacuum evaporation process variables. Process Biochemistry, 38( 8), 1231-1237. doi:10.1016/s0032-9592(02)00290-x
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      Rodrigues R de CLB, Felipe M das G de A, Silva JB de A e, Vitolo M. Response surface methodology for xylitol production from sugarcane bagasse hemicellulosic hydrolyzate using controlled vacuum evaporation process variables [Internet]. Process Biochemistry. 2003 ; 38( 8): 1231-1237.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/s0032-9592(02)00290-x
    • Vancouver

      Rodrigues R de CLB, Felipe M das G de A, Silva JB de A e, Vitolo M. Response surface methodology for xylitol production from sugarcane bagasse hemicellulosic hydrolyzate using controlled vacuum evaporation process variables [Internet]. Process Biochemistry. 2003 ; 38( 8): 1231-1237.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/s0032-9592(02)00290-x
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BIOQUÍMICA, BIOTECNOLOGIA, PROTEÍNAS

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      RICCI-SILVA, M. E. e VITOLO, Michele e ABRAHÃO NETO, José. Protein and glucose 6-phosphate dehydrogenase releasing from baker´s yeast cells disrupted by a vertical bead mill. Process Biochemistry, v. 35, n. 18, p. 831-835, 2000Tradução . . Disponível em: https://doi.org/10.1016/s0032-9592(99)00151-x. Acesso em: 30 set. 2024.
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      Ricci-Silva, M. E., Vitolo, M., & Abrahão Neto, J. (2000). Protein and glucose 6-phosphate dehydrogenase releasing from baker´s yeast cells disrupted by a vertical bead mill. Process Biochemistry, 35( 18), 831-835. doi:10.1016/s0032-9592(99)00151-x
    • NLM

      Ricci-Silva ME, Vitolo M, Abrahão Neto J. Protein and glucose 6-phosphate dehydrogenase releasing from baker´s yeast cells disrupted by a vertical bead mill [Internet]. Process Biochemistry. 2000 ; 35( 18): 831-835.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/s0032-9592(99)00151-x
    • Vancouver

      Ricci-Silva ME, Vitolo M, Abrahão Neto J. Protein and glucose 6-phosphate dehydrogenase releasing from baker´s yeast cells disrupted by a vertical bead mill [Internet]. Process Biochemistry. 2000 ; 35( 18): 831-835.[citado 2024 set. 30 ] Available from: https://doi.org/10.1016/s0032-9592(99)00151-x

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