Filtros : "Estados Unidos" "Squina, Fabio M." "POLIKARPOV, IGOR" Removido: "SW" Limpar

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  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS

    Acesso à fonteDOIHow to cite
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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: 22 dez. 2024.
    • 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 2024 dez. 22 ] 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 2024 dez. 22 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
  • Source: Genome Announcements. Unidade: IFSC

    Subjects: BIOTECNOLOGIA, TUBERCULOSE

    Acesso à fonteDOIHow to cite
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    • ABNT

      MANDELLI, Fernanda et al. Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest. Genome Announcements, v. 3, n. 3, p. e00475-15-1-e00475-15-2, 2015Tradução . . Disponível em: https://doi.org/10.1128/genomeA.00466-15. Acesso em: 22 dez. 2024.
    • APA

      Mandelli, F., Ramires, B. O., Couger, M. B., Paixão, D. A. A., Camilo, C. M., Polikarpov, I., et al. (2015). Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest. Genome Announcements, 3( 3), e00475-15-1-e00475-15-2. doi:10.1128/genomeA.00466-15
    • NLM

      Mandelli F, Ramires BO, Couger MB, Paixão DAA, Camilo CM, Polikarpov I, Prade R, Riaño-Pachón DM, Squina FM. Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest [Internet]. Genome Announcements. 2015 ; 3( 3): e00475-15-1-e00475-15-2.[citado 2024 dez. 22 ] Available from: https://doi.org/10.1128/genomeA.00466-15
    • Vancouver

      Mandelli F, Ramires BO, Couger MB, Paixão DAA, Camilo CM, Polikarpov I, Prade R, Riaño-Pachón DM, Squina FM. Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest [Internet]. Genome Announcements. 2015 ; 3( 3): e00475-15-1-e00475-15-2.[citado 2024 dez. 22 ] Available from: https://doi.org/10.1128/genomeA.00466-15
  • Source: Journal of Biological Chemistry. Unidade: IFSC

    Subjects: ENZIMAS, BIOQUÍMICA

    Acesso à fonteDOIHow to cite
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    • ABNT

      LIMA, Marisa A. et al. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function. Journal of Biological Chemistry, v. No 2013, n. 46, p. 32991-33005, 2013Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.479279. Acesso em: 22 dez. 2024.
    • APA

      Lima, M. A., Oliveira Neto, M., Kadowaki, M. A. S., Rosseto, F. R., Prates, E. T., Squina, F. M., et al. (2013). Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function. Journal of Biological Chemistry, No 2013( 46), 32991-33005. doi:10.1074/jbc.M113.479279
    • NLM

      Lima MA, Oliveira Neto M, Kadowaki MAS, Rosseto FR, Prates ET, Squina FM, Leme AFP, Skaf MS, Polikarpov I. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function [Internet]. Journal of Biological Chemistry. 2013 ; No 2013( 46): 32991-33005.[citado 2024 dez. 22 ] Available from: https://doi.org/10.1074/jbc.M113.479279
    • Vancouver

      Lima MA, Oliveira Neto M, Kadowaki MAS, Rosseto FR, Prates ET, Squina FM, Leme AFP, Skaf MS, Polikarpov I. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function [Internet]. Journal of Biological Chemistry. 2013 ; No 2013( 46): 32991-33005.[citado 2024 dez. 22 ] Available from: https://doi.org/10.1074/jbc.M113.479279

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