Filtros : "Araújo, Evandro Ares de" "Polikarpov, Igor" "2024" Limpar

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  • Source: Carbohydrate Polymers. Unidade: IFSC

    Subjects: GLICOSÍDEOS, ENZIMAS HIDROLÍTICAS, CARBOIDRATOS, POLISSACARÍDEOS

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    • ABNT

      ARAÚJO, Evandro Ares de et al. Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family 9. Carbohydrate Polymers, v. 329, p. 121739-1-121739-18 + supplementary data: 1-11, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.carbpol.2023.121739. Acesso em: 17 nov. 2024.
    • APA

      Araújo, E. A. de, Cortez, A. A., Pellegrini, V. de O. A., Vacilotto, M. M., Cruz, A. F., Batista, P. R., & Polikarpov, I. (2024). Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family 9. Carbohydrate Polymers, 329, 121739-1-121739-18 + supplementary data: 1-11. doi:10.1016/j.carbpol.2023.121739
    • NLM

      Araújo EA de, Cortez AA, Pellegrini V de OA, Vacilotto MM, Cruz AF, Batista PR, Polikarpov I. Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family 9 [Internet]. Carbohydrate Polymers. 2024 ; 329 121739-1-121739-18 + supplementary data: 1-11.[citado 2024 nov. 17 ] Available from: https://doi.org/10.1016/j.carbpol.2023.121739
    • Vancouver

      Araújo EA de, Cortez AA, Pellegrini V de OA, Vacilotto MM, Cruz AF, Batista PR, Polikarpov I. Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family 9 [Internet]. Carbohydrate Polymers. 2024 ; 329 121739-1-121739-18 + supplementary data: 1-11.[citado 2024 nov. 17 ] Available from: https://doi.org/10.1016/j.carbpol.2023.121739
  • Source: International Journal of Biological Macromolecules. Unidade: IFSC

    Subjects: AÇUCARES, ENZIMAS, BIOTECNOLOGIA, CRISTALOGRAFIA ESTRUTURAL

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    • ABNT

      BRIGANTI, Lorenzo et al. Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies. International Journal of Biological Macromolecules, v. 274, p. 133182-1-133182-16 + supplementary data, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2024.133182. Acesso em: 17 nov. 2024.
    • APA

      Briganti, L., Manzine, L. R., Capetti, C. C. de M., Araújo, E. A. de, Pellegrini, V. de O. A., Guimarães, F. E. G., et al. (2024). Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies. International Journal of Biological Macromolecules, 274, 133182-1-133182-16 + supplementary data. doi:10.1016/j.ijbiomac.2024.133182
    • NLM

      Briganti L, Manzine LR, Capetti CC de M, Araújo EA de, Pellegrini V de OA, Guimarães FEG, Oliveira Neto M de, Polikarpov I. Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies [Internet]. International Journal of Biological Macromolecules. 2024 ; 274 133182-1-133182-16 + supplementary data.[citado 2024 nov. 17 ] Available from: https://doi.org/10.1016/j.ijbiomac.2024.133182
    • Vancouver

      Briganti L, Manzine LR, Capetti CC de M, Araújo EA de, Pellegrini V de OA, Guimarães FEG, Oliveira Neto M de, Polikarpov I. Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies [Internet]. International Journal of Biological Macromolecules. 2024 ; 274 133182-1-133182-16 + supplementary data.[citado 2024 nov. 17 ] Available from: https://doi.org/10.1016/j.ijbiomac.2024.133182
  • Source: Carbohydrate Polymers. Unidade: IFSC

    Subjects: ENZIMAS, POLISSACARÍDEOS, BIOTECNOLOGIA

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    • ABNT

      VACILOTTO, Milena Moreira et al. Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase. Carbohydrate Polymers, v. 337, p. 122141-1-122141-14 + supplementary data, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.carbpol.2024.122141. Acesso em: 17 nov. 2024.
    • APA

      Vacilotto, M. M., Montalvão, L. de A., Pellegrini, V. de O. A., Liberato, M. V., Araújo, E. A. de, & Polikarpov, I. (2024). Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase. Carbohydrate Polymers, 337, 122141-1-122141-14 + supplementary data. doi:10.1016/j.carbpol.2024.122141
    • NLM

      Vacilotto MM, Montalvão L de A, Pellegrini V de OA, Liberato MV, Araújo EA de, Polikarpov I. Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase [Internet]. Carbohydrate Polymers. 2024 ; 337 122141-1-122141-14 + supplementary data.[citado 2024 nov. 17 ] Available from: https://doi.org/10.1016/j.carbpol.2024.122141
    • Vancouver

      Vacilotto MM, Montalvão L de A, Pellegrini V de OA, Liberato MV, Araújo EA de, Polikarpov I. Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase [Internet]. Carbohydrate Polymers. 2024 ; 337 122141-1-122141-14 + supplementary data.[citado 2024 nov. 17 ] Available from: https://doi.org/10.1016/j.carbpol.2024.122141

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