Filtros : "Enzyme and Microbial Technology" "HIDRÓLISE" Limpar

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  • Source: Enzyme and Microbial Technology. Unidade: FFCLRP

    Subjects: BIOMASSA, ENZIMAS, EXPRESSÃO GÊNICA, HIDRÓLISE, LIGNINA, PROTEÍNAS, ENGENHARIA, PROTEÍNAS RECOMBINANTES

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    • ABNT

      MARTINS, Manoela e DINAMARCO, Taisa Magnani e GOLDBECK, Rosana. Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis. Enzyme and Microbial Technology, v. 140, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2020.109647. Acesso em: 12 dez. 2025.
    • APA

      Martins, M., Dinamarco, T. M., & Goldbeck, R. (2020). Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis. Enzyme and Microbial Technology, 140. doi:10.1016/j.enzmictec.2020.109647
    • NLM

      Martins M, Dinamarco TM, Goldbeck R. Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis [Internet]. Enzyme and Microbial Technology. 2020 ; 140[citado 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2020.109647
    • Vancouver

      Martins M, Dinamarco TM, Goldbeck R. Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis [Internet]. Enzyme and Microbial Technology. 2020 ; 140[citado 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2020.109647
  • Source: Enzyme and Microbial Technology. Unidades: IFSC, EEL

    Subjects: CANA-DE-AÇÚCAR, BAGAÇOS, HIDRÓLISE

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    • ABNT

      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: 12 dez. 2025.
    • APA

      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
    • NLM

      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 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
    • Vancouver

      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 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS

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    • ABNT

      SILVA, Viviam M. et al. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, v. 87-88, p. 1-8, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2016.02.007. Acesso em: 12 dez. 2025.
    • APA

      Silva, V. M., Souza, A. S., Negrão, D. R., Polikarpov, I., Squina, F. M., Oliveira Neto, M. de, et al. (2016). Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, 87-88, 1-8. doi:10.1016/j.enzmictec.2016.02.007
    • NLM

      Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
    • Vancouver

      Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: ENZIMAS, HIDRÓLISE, XANTHOMONAS

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    • ABNT

      ROSSETO, Flávio Rodolfo et al. Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris. Enzyme and Microbial Technology, v. 91, p. 1-7, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2016.05.007. Acesso em: 12 dez. 2025.
    • APA

      Rosseto, F. R., Manzine, L. R., Oliveira Neto, M. de, & Polikarpov, I. (2016). Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris. Enzyme and Microbial Technology, 91, 1-7. doi:10.1016/j.enzmictec.2016.05.007
    • NLM

      Rosseto FR, Manzine LR, Oliveira Neto M de, Polikarpov I. Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris [Internet]. Enzyme and Microbial Technology. 2016 ; 91 1-7.[citado 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.05.007
    • Vancouver

      Rosseto FR, Manzine LR, Oliveira Neto M de, Polikarpov I. Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris [Internet]. Enzyme and Microbial Technology. 2016 ; 91 1-7.[citado 2025 dez. 12 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.05.007

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