Filtros : "Cellulase" Limpar

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  • Source: Chemical engineering journal. Unidade: EEL

    Subjects: BIOTECNOLOGIA, CELULOSE

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      REIS, Cristiano E. Rodrigues et al. Process strategies to reduce cellulase enzyme loading for renewable sugar production in biorefineries. Chemical engineering journal, v. 451, p. 138690-138700, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.cej.2022.138690. Acesso em: 04 jan. 2026.
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      Reis, C. E. R., Libardi Junior, N., Bento, H. B. S., Carvalho, A. K. F. de, Vandenberghe, L. P. de S., Soccol, C. R., et al. (2022). Process strategies to reduce cellulase enzyme loading for renewable sugar production in biorefineries. Chemical engineering journal, 451, 138690-138700. doi:10.1016/j.cej.2022.138690
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      Reis CER, Libardi Junior N, Bento HBS, Carvalho AKF de, Vandenberghe LP de S, Soccol CR, Aminabhavi TM, Chandel AK. Process strategies to reduce cellulase enzyme loading for renewable sugar production in biorefineries [Internet]. Chemical engineering journal. 2022 ;451 138690-138700.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.cej.2022.138690
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      Reis CER, Libardi Junior N, Bento HBS, Carvalho AKF de, Vandenberghe LP de S, Soccol CR, Aminabhavi TM, Chandel AK. Process strategies to reduce cellulase enzyme loading for renewable sugar production in biorefineries [Internet]. Chemical engineering journal. 2022 ;451 138690-138700.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.cej.2022.138690
  • Source: Protoplasma. Unidade: FCFRP

    Subjects: CANNABIS, FLORES, LATEX, MORFOLOGIA VEGETAL, METABÓLITOS SECUNDÁRIOS, CANABINOIDES, PROTOPLASMA

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      LEME, Flávia Maria et al. Expanding the laticifer knowledge in Cannabaceae: distribution, morphology, origin, and latex composition. Protoplasma, v. 257, n. 4, p. 1183-1199, 2020Tradução . . Disponível em: https://doi.org/10.1007/s00709-020-01500-5. Acesso em: 04 jan. 2026.
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      Leme, F. M., Borella, P. H., Marinho, C. R., & Teixeira, S. de P. (2020). Expanding the laticifer knowledge in Cannabaceae: distribution, morphology, origin, and latex composition. Protoplasma, 257( 4), 1183-1199. doi:10.1007/s00709-020-01500-5
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      Leme FM, Borella PH, Marinho CR, Teixeira S de P. Expanding the laticifer knowledge in Cannabaceae: distribution, morphology, origin, and latex composition [Internet]. Protoplasma. 2020 ; 257( 4): 1183-1199.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1007/s00709-020-01500-5
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      Leme FM, Borella PH, Marinho CR, Teixeira S de P. Expanding the laticifer knowledge in Cannabaceae: distribution, morphology, origin, and latex composition [Internet]. Protoplasma. 2020 ; 257( 4): 1183-1199.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1007/s00709-020-01500-5
  • Source: Enzyme and Microbial Technology. Unidades: IFSC, EEL

    Subjects: CANA-DE-AÇÚCAR, BAGAÇOS, HIDRÓLISE

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      BERTO, Gabriela Leila et al. Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45. Enzyme and Microbial Technology, v. 120, n. Ja 2019, p. 23-35, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2018.09.005. Acesso em: 04 jan. 2026.
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      Berto, G. L., Velasco, J., Ribeiro, C. T. C., Zanphorlin, L. M., Domingues, M. N., Murakami, M. T., et al. (2019). Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45. Enzyme and Microbial Technology, 120( Ja 2019), 23-35. doi:10.1016/j.enzmictec.2018.09.005
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      Berto GL, Velasco J, Ribeiro CTC, Zanphorlin LM, Domingues MN, Murakami MT, Polikarpov I, Oliveira LC de, Ferraz A, Segato F. Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45 [Internet]. Enzyme and Microbial Technology. 2019 ; 120( Ja 2019): 23-35.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
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      Berto GL, Velasco J, Ribeiro CTC, Zanphorlin LM, Domingues MN, Murakami MT, Polikarpov I, Oliveira LC de, Ferraz A, Segato F. Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45 [Internet]. Enzyme and Microbial Technology. 2019 ; 120( Ja 2019): 23-35.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
  • Source: Biochimica et Biophysica Acta: General Subjects. Unidade: IFSC

    Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE

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      SONODA, Milton T. et al. Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides. Biochimica et Biophysica Acta: General Subjects, v. 1863, n. 6, p. 1015-1026, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.bbagen.2019.03.013. Acesso em: 04 jan. 2026.
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      Sonoda, M. T., Godoy, A. S., Pellegrini, V. O. A., Kadowaki, M. A. S., Nascimento, A. S., & Polikarpov, I. (2019). Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides. Biochimica et Biophysica Acta: General Subjects, 1863( 6), 1015-1026. doi:10.1016/j.bbagen.2019.03.013
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      Sonoda MT, Godoy AS, Pellegrini VOA, Kadowaki MAS, Nascimento AS, Polikarpov I. Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides [Internet]. Biochimica et Biophysica Acta: General Subjects. 2019 ; 1863( 6): 1015-1026.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.bbagen.2019.03.013
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      Sonoda MT, Godoy AS, Pellegrini VOA, Kadowaki MAS, Nascimento AS, Polikarpov I. Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides [Internet]. Biochimica et Biophysica Acta: General Subjects. 2019 ; 1863( 6): 1015-1026.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.bbagen.2019.03.013
  • Source: Matéria (Rio de Janeiro). Unidade: FFCLRP

    Subjects: ALGAS, BIOMASSA, CÉLULAS, RHODOPHYTA, CLOSTRIDIUM

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      RODRIGUES, Emelin Leandro et al. Enzymatically and/or thermally treated Macroalgae biomass as feedstock for fermentative H2 production. Matéria (Rio de Janeiro), v. 24, n. 2, 2019Tradução . . Disponível em: https://doi.org/10.1590/s1517-707620190002.0678. Acesso em: 04 jan. 2026.
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      Rodrigues, E. L., Fonseca, B. C., Gelli, V. C., Carli, S., Meleiro, L. P., Furriel, R. dos P. M., & Reginatto, V. (2019). Enzymatically and/or thermally treated Macroalgae biomass as feedstock for fermentative H2 production. Matéria (Rio de Janeiro), 24( 2). doi:10.1590/s1517-707620190002.0678
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      Rodrigues EL, Fonseca BC, Gelli VC, Carli S, Meleiro LP, Furriel R dos PM, Reginatto V. Enzymatically and/or thermally treated Macroalgae biomass as feedstock for fermentative H2 production [Internet]. Matéria (Rio de Janeiro). 2019 ; 24( 2):[citado 2026 jan. 04 ] Available from: https://doi.org/10.1590/s1517-707620190002.0678
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      Rodrigues EL, Fonseca BC, Gelli VC, Carli S, Meleiro LP, Furriel R dos PM, Reginatto V. Enzymatically and/or thermally treated Macroalgae biomass as feedstock for fermentative H2 production [Internet]. Matéria (Rio de Janeiro). 2019 ; 24( 2):[citado 2026 jan. 04 ] Available from: https://doi.org/10.1590/s1517-707620190002.0678
  • Source: Biotechnology for Biofuels. Unidades: FCFRP, FMRP

    Subjects: BIOCOMBUSTÍVEIS, SACCHAROMYCES, BAGAÇOS, CANA-DE-AÇÚCAR, TRICHODERMA

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      NOGUEIRA, Karoline M. V. et al. Characterization of a novel sugar transporter involved in sugarcane bagasse degradation in Trichoderma reesei. Biotechnology for Biofuels, v. 11, 2018Tradução . . Disponível em: https://doi.org/10.1186/s13068-018-1084-1. Acesso em: 04 jan. 2026.
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      Nogueira, K. M. V., Paula, R. G. de, Antoniêto, A. C. C., Reis, T. F. dos, Carraro, C. B., Silva, A. C., et al. (2018). Characterization of a novel sugar transporter involved in sugarcane bagasse degradation in Trichoderma reesei. Biotechnology for Biofuels, 11. doi:10.1186/s13068-018-1084-1
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      Nogueira KMV, Paula RG de, Antoniêto ACC, Reis TF dos, Carraro CB, Silva AC, Almeida F, Rechia CGV, Goldman GH, Silva RN. Characterization of a novel sugar transporter involved in sugarcane bagasse degradation in Trichoderma reesei [Internet]. Biotechnology for Biofuels. 2018 ; 11[citado 2026 jan. 04 ] Available from: https://doi.org/10.1186/s13068-018-1084-1
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      Nogueira KMV, Paula RG de, Antoniêto ACC, Reis TF dos, Carraro CB, Silva AC, Almeida F, Rechia CGV, Goldman GH, Silva RN. Characterization of a novel sugar transporter involved in sugarcane bagasse degradation in Trichoderma reesei [Internet]. Biotechnology for Biofuels. 2018 ; 11[citado 2026 jan. 04 ] Available from: https://doi.org/10.1186/s13068-018-1084-1
  • Source: International Journal of Biological Macromolecules. Unidade: IFSC

    Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE

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      ARAÚJO, Evandro Ares de et al. Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis. International Journal of Biological Macromolecules, v. 111, p. 302-310, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.12.138. Acesso em: 04 jan. 2026.
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      Araújo, E. A. de, Manzine, L. R., Piiadov, V., Kadowaki, M. A. S., & Polikarpov, I. (2018). Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis. International Journal of Biological Macromolecules, 111, 302-310. doi:10.1016/j.ijbiomac.2017.12.138
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      Araújo EA de, Manzine LR, Piiadov V, Kadowaki MAS, Polikarpov I. Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis [Internet]. International Journal of Biological Macromolecules. 2018 ; 111 302-310.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.138
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      Araújo EA de, Manzine LR, Piiadov V, Kadowaki MAS, Polikarpov I. Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis [Internet]. International Journal of Biological Macromolecules. 2018 ; 111 302-310.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.138
  • Source: Biotechnology for Biofuels. Unidade: FCFRP

    Subjects: ETANOL, CELULOSE, ENZIMAS CELULOLÍTICAS, TRICHODERMA, MELAÇO, CASCAS (PLANTA)

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      ELLILÄ, Simo et al. Development of a low-cost cellulase production process using Trichoderma reesei for Brazilian biorefineries. Biotechnology for Biofuels, v. 10, n. 1, 2017Tradução . . Disponível em: https://doi.org/10.1186/s13068-017-0717-0. Acesso em: 04 jan. 2026.
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      Ellilä, S., Fonseca, L., Uchima, C., Cota, J., Goldman, G. H., Saloheimo, M., et al. (2017). Development of a low-cost cellulase production process using Trichoderma reesei for Brazilian biorefineries. Biotechnology for Biofuels, 10( 1). doi:10.1186/s13068-017-0717-0
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      Ellilä S, Fonseca L, Uchima C, Cota J, Goldman GH, Saloheimo M, Sacon V, Siika-aho M. Development of a low-cost cellulase production process using Trichoderma reesei for Brazilian biorefineries [Internet]. Biotechnology for Biofuels. 2017 ; 10( 1):[citado 2026 jan. 04 ] Available from: https://doi.org/10.1186/s13068-017-0717-0
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      Ellilä S, Fonseca L, Uchima C, Cota J, Goldman GH, Saloheimo M, Sacon V, Siika-aho M. Development of a low-cost cellulase production process using Trichoderma reesei for Brazilian biorefineries [Internet]. Biotechnology for Biofuels. 2017 ; 10( 1):[citado 2026 jan. 04 ] Available from: https://doi.org/10.1186/s13068-017-0717-0
  • Source: Abstracts. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Subjects: ENZIMAS CELULOLÍTICAS, BIOMATERIAIS

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      LIBERATO, M. V. et al. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism. 2016, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2016. Disponível em: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm. Acesso em: 04 jan. 2026.
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      Liberato, M. V., Silveira, R. L., Prates, E. T., Araujo, E. A., Pellegrini, V. O. A., Camilo, C. M., et al. (2016). Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
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      Liberato MV, Silveira RL, Prates ET, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism [Internet]. Abstracts. 2016 ;[citado 2026 jan. 04 ] Available from: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
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      Liberato MV, Silveira RL, Prates ET, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism [Internet]. Abstracts. 2016 ;[citado 2026 jan. 04 ] Available from: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
  • Source: Biotechnology Progress. Unidade: IFSC

    Subjects: BAGAÇOS, CANA-DE-AÇÚCAR, CELULOSE, HIDRÓLISE, ENZIMAS

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      ARIAS, Johanna Méndez et al. Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies. Biotechnology Progress, v. 32, n. 5, p. 1222-1229, 2016Tradução . . Disponível em: https://doi.org/10.1002/btpr.2306. Acesso em: 04 jan. 2026.
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      Arias, J. M., Modesto, L. F. A., Polikarpov, I., & Pereira Junior, N. (2016). Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies. Biotechnology Progress, 32( 5), 1222-1229. doi:10.1002/btpr.2306
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      Arias JM, Modesto LFA, Polikarpov I, Pereira Junior N. Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies [Internet]. Biotechnology Progress. 2016 ; 32( 5): 1222-1229.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1002/btpr.2306
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      Arias JM, Modesto LFA, Polikarpov I, Pereira Junior N. Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies [Internet]. Biotechnology Progress. 2016 ; 32( 5): 1222-1229.[citado 2026 jan. 04 ] Available from: https://doi.org/10.1002/btpr.2306
  • Unidade: IFSC

    Subjects: ENZIMAS (ESTUDO), CRISTALOGRAFIA, CELULOSE

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      RAMIA, Marina Paglione. Estudos funcionais e estruturais de uma endoglucanase de Phanerochaete chrysosporium da família 45 das hidrolases de glicosídeos. 2015. Tese (Doutorado) – Universidade de São Paulo, São Carlos, 2015. Disponível em: http://www.teses.usp.br/teses/disponiveis/76/76132/tde-10032016-150356/. Acesso em: 04 jan. 2026.
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      Ramia, M. P. (2015). Estudos funcionais e estruturais de uma endoglucanase de Phanerochaete chrysosporium da família 45 das hidrolases de glicosídeos (Tese (Doutorado). Universidade de São Paulo, São Carlos. Recuperado de http://www.teses.usp.br/teses/disponiveis/76/76132/tde-10032016-150356/
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      Ramia MP. Estudos funcionais e estruturais de uma endoglucanase de Phanerochaete chrysosporium da família 45 das hidrolases de glicosídeos [Internet]. 2015 ;[citado 2026 jan. 04 ] Available from: http://www.teses.usp.br/teses/disponiveis/76/76132/tde-10032016-150356/
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      Ramia MP. Estudos funcionais e estruturais de uma endoglucanase de Phanerochaete chrysosporium da família 45 das hidrolases de glicosídeos [Internet]. 2015 ;[citado 2026 jan. 04 ] Available from: http://www.teses.usp.br/teses/disponiveis/76/76132/tde-10032016-150356/

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