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  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: BIOFÍSICA, ENZIMAS, BIOTECNOLOGIA, SUSTENTABILIDADE

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    • ABNT

      ALMEIDA, Dnane Vieira et al. Unveiling the crystal structure of thermostable dienelactone hydrolase exhibiting activity on terephthalate esters. Enzyme and Microbial Technology, v. 180, p. 110498-1-110498-10 + supplementary material, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2024.110498. Acesso em: 01 nov. 2024.
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      Almeida, D. V., Ciancaglini, I., Sandano, A. L. H., Roman, E. K. B., Andrade, V. B., Nunes, A. B., et al. (2024). Unveiling the crystal structure of thermostable dienelactone hydrolase exhibiting activity on terephthalate esters. Enzyme and Microbial Technology, 180, 110498-1-110498-10 + supplementary material. doi:10.1016/j.enzmictec.2022.1100198
    • NLM

      Almeida DV, Ciancaglini I, Sandano ALH, Roman EKB, Andrade VB, Nunes AB, Tramontina R, Silva VM da, Gabel F, Corrêa TLR, Damásio AR de L, Muniz JRC, Squina FM, Garcia WJ. Unveiling the crystal structure of thermostable dienelactone hydrolase exhibiting activity on terephthalate esters [Internet]. Enzyme and Microbial Technology. 2024 ; 180 110498-1-110498-10 + supplementary material.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2024.110498
    • Vancouver

      Almeida DV, Ciancaglini I, Sandano ALH, Roman EKB, Andrade VB, Nunes AB, Tramontina R, Silva VM da, Gabel F, Corrêa TLR, Damásio AR de L, Muniz JRC, Squina FM, Garcia WJ. Unveiling the crystal structure of thermostable dienelactone hydrolase exhibiting activity on terephthalate esters [Internet]. Enzyme and Microbial Technology. 2024 ; 180 110498-1-110498-10 + supplementary material.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2024.110498
  • Source: Enzyme and Microbial Technology. Unidade: EESC

    Subjects: BAGAÇOS, REATORES ANAERÓBIOS, CANA-DE-AÇÚCAR, ENGENHARIA HIDRÁULICA

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      RABELO, Camila Abreu Borges da Silva et al. Metataxonomic characterization of an autochthonous and allochthonous microbial consortium involved in a two-stage anaerobic batch reactor applied to hydrogen and methane production from sugarcane bagasse. Enzyme and Microbial Technology, v. 162, p. 1-11, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2022.110119. Acesso em: 01 nov. 2024.
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      Rabelo, C. A. B. da S., Camargo, F. P., Sakamoto, I. K., & Varesche, M. B. A. (2023). Metataxonomic characterization of an autochthonous and allochthonous microbial consortium involved in a two-stage anaerobic batch reactor applied to hydrogen and methane production from sugarcane bagasse. Enzyme and Microbial Technology, 162, 1-11. doi:10.1016/j.enzmictec.2022.110119
    • NLM

      Rabelo CAB da S, Camargo FP, Sakamoto IK, Varesche MBA. Metataxonomic characterization of an autochthonous and allochthonous microbial consortium involved in a two-stage anaerobic batch reactor applied to hydrogen and methane production from sugarcane bagasse [Internet]. Enzyme and Microbial Technology. 2023 ; 162 1-11.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2022.110119
    • Vancouver

      Rabelo CAB da S, Camargo FP, Sakamoto IK, Varesche MBA. Metataxonomic characterization of an autochthonous and allochthonous microbial consortium involved in a two-stage anaerobic batch reactor applied to hydrogen and methane production from sugarcane bagasse [Internet]. Enzyme and Microbial Technology. 2023 ; 162 1-11.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2022.110119
  • Source: Enzyme and Microbial Technology. Unidades: CENA, RUSP, FFCLRP, FMRP

    Subjects: ENZIMAS, MONOSSACARÍDEOS

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      BARRETO, Matheus Quintana et al. Xylose isomerase from Piromyces sp. E2 is a promiscuous enzyme with epimerase activity. Enzyme and Microbial Technology, v. 166, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2023.110230. Acesso em: 01 nov. 2024.
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      Barreto, M. Q., Garbelotti, C. V., Soares, J. de M., Grandis, A., Buckeridge, M., Leone, F. de A., & Ward, R. J. (2023). Xylose isomerase from Piromyces sp. E2 is a promiscuous enzyme with epimerase activity. Enzyme and Microbial Technology, 166. doi:10.1016/j.enzmictec.2023.110230
    • NLM

      Barreto MQ, Garbelotti CV, Soares J de M, Grandis A, Buckeridge M, Leone F de A, Ward RJ. Xylose isomerase from Piromyces sp. E2 is a promiscuous enzyme with epimerase activity [Internet]. Enzyme and Microbial Technology. 2023 ; 166[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2023.110230
    • Vancouver

      Barreto MQ, Garbelotti CV, Soares J de M, Grandis A, Buckeridge M, Leone F de A, Ward RJ. Xylose isomerase from Piromyces sp. E2 is a promiscuous enzyme with epimerase activity [Internet]. Enzyme and Microbial Technology. 2023 ; 166[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2023.110230
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: MATERIAIS NANOESTRUTURADOS, NANOPARTÍCULAS, BIOTECNOLOGIA

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      SABI, Guilherme J. et al. Decyl esters production from soybean-based oils catalyzed by lipase immobilized on differently functionalized rice husk silica and their characterization as potential biolubricants. Enzyme and Microbial Technology, v. 157, p. 110019-1-110019-14, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2022.110019. Acesso em: 01 nov. 2024.
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      Sabi, G. J., Gama, R. S., Fernandez-Lafuente, R., Bernardi, J. C., & Mendes, A. A. (2022). Decyl esters production from soybean-based oils catalyzed by lipase immobilized on differently functionalized rice husk silica and their characterization as potential biolubricants. Enzyme and Microbial Technology, 157, 110019-1-110019-14. doi:10.1016/j.enzmictec.2022.110019
    • NLM

      Sabi GJ, Gama RS, Fernandez-Lafuente R, Bernardi JC, Mendes AA. Decyl esters production from soybean-based oils catalyzed by lipase immobilized on differently functionalized rice husk silica and their characterization as potential biolubricants [Internet]. Enzyme and Microbial Technology. 2022 ; 157 110019-1-110019-14.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2022.110019
    • Vancouver

      Sabi GJ, Gama RS, Fernandez-Lafuente R, Bernardi JC, Mendes AA. Decyl esters production from soybean-based oils catalyzed by lipase immobilized on differently functionalized rice husk silica and their characterization as potential biolubricants [Internet]. Enzyme and Microbial Technology. 2022 ; 157 110019-1-110019-14.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2022.110019
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: BIOTECNOLOGIA, BIOMASSA, ENZIMAS

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      VACILOTTO, Milena Moreira et al. Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family. Enzyme and Microbial Technology, v. 144, p. 109743-1-109743-9, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2021.109743. Acesso em: 01 nov. 2024.
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      Vacilotto, M. M., Sepulchro, A. G. V., Pellegrini, V. de O. A., & Polikarpov, I. (2021). Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family. Enzyme and Microbial Technology, 144, 109743-1-109743-9. doi:10.1016/j.enzmictec.2021.109743
    • NLM

      Vacilotto MM, Sepulchro AGV, Pellegrini V de OA, Polikarpov I. Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family [Internet]. Enzyme and Microbial Technology. 2021 ; 144 109743-1-109743-9.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2021.109743
    • Vancouver

      Vacilotto MM, Sepulchro AGV, Pellegrini V de OA, Polikarpov I. Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family [Internet]. Enzyme and Microbial Technology. 2021 ; 144 109743-1-109743-9.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2021.109743
  • Source: Enzyme and Microbial Technology. Unidades: IFSC, EEL, BIOENERGIA

    Subjects: BIOTECNOLOGIA, BIOMASSA, ENZIMAS, SACARIFICAÇÃO, CANA-DE-AÇÚCAR, FUNGOS TERMÓFILOS, ASPERGILLUS

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      VELASCO, Josman et al. Comparative analysis of two recombinant LPMOs from Aspergillus fumigatus and their effects on sugarcane bagasse saccharification. Enzyme and Microbial Technology, v. 144, p. 109746-1-109746-11 1 + supplementary data, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2021.109746. Acesso em: 01 nov. 2024.
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      Velasco, J., Pellegrini, V. de O. A., Sepulchro, A. G. V., Kadowakic, M. A. S., Espirito Santo, M. C. do, Polikarpov, I., & Segato, F. (2021). Comparative analysis of two recombinant LPMOs from Aspergillus fumigatus and their effects on sugarcane bagasse saccharification. Enzyme and Microbial Technology, 144, 109746-1-109746-11 1 + supplementary data. doi:10.1016/j.enzmictec.2021.109746
    • NLM

      Velasco J, Pellegrini V de OA, Sepulchro AGV, Kadowakic MAS, Espirito Santo MC do, Polikarpov I, Segato F. Comparative analysis of two recombinant LPMOs from Aspergillus fumigatus and their effects on sugarcane bagasse saccharification [Internet]. Enzyme and Microbial Technology. 2021 ; 144 109746-1-109746-11 1 + supplementary data.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2021.109746
    • Vancouver

      Velasco J, Pellegrini V de OA, Sepulchro AGV, Kadowakic MAS, Espirito Santo MC do, Polikarpov I, Segato F. Comparative analysis of two recombinant LPMOs from Aspergillus fumigatus and their effects on sugarcane bagasse saccharification [Internet]. Enzyme and Microbial Technology. 2021 ; 144 109746-1-109746-11 1 + supplementary data.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2021.109746
  • Source: Enzyme and Microbial Technology. Unidade: FFCLRP

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

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      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: 01 nov. 2024.
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      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 2024 nov. 01 ] 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 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2020.109647
  • Source: Enzyme and Microbial Technology. Unidades: EACH, FOB, FCF, IQ

    Subjects: ENZIMAS, MATERIAIS NANOESTRUTURADOS, CELULOSE, BAGAÇOS, CANA-DE-AÇÚCAR

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      BRITES, Mariana de Melo et al. Bromelain immobilization in cellulose triacetate nanofiber membranes from sugarcane bagasse by electrospinning technique. Enzyme and Microbial Technology, v. 132, n. Ja 2020, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2019.109384. Acesso em: 01 nov. 2024.
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      Brites, M. de M., Cerón, A. A., Costa, S. M. da, Oliveira, R. C. de, Ferraz, H. G., Catalani, L. H., & Costa, S. A. da. (2020). Bromelain immobilization in cellulose triacetate nanofiber membranes from sugarcane bagasse by electrospinning technique. Enzyme and Microbial Technology, 132( Ja 2020). doi:10.1016/j.enzmictec.2019.109384
    • NLM

      Brites M de M, Cerón AA, Costa SM da, Oliveira RC de, Ferraz HG, Catalani LH, Costa SA da. Bromelain immobilization in cellulose triacetate nanofiber membranes from sugarcane bagasse by electrospinning technique [Internet]. Enzyme and Microbial Technology. 2020 ; 132( Ja 2020):[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2019.109384
    • Vancouver

      Brites M de M, Cerón AA, Costa SM da, Oliveira RC de, Ferraz HG, Catalani LH, Costa SA da. Bromelain immobilization in cellulose triacetate nanofiber membranes from sugarcane bagasse by electrospinning technique [Internet]. Enzyme and Microbial Technology. 2020 ; 132( Ja 2020):[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2019.109384
  • 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: 01 nov. 2024.
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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
    • 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 2024 nov. 01 ] 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 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
  • Source: Enzyme and Microbial Technology. Unidade: ESALQ

    Subjects: ANTIOXIDANTES, ASPERGILLUS, COMPOSTOS FENÓLICOS, ENZIMAS

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      MONCLARO, Antonielle Vieira et al. Xylanase from Aspergillus tamarii shows different kinetic parameters and substrate specificity in the presence of ferulic acid. Enzyme and Microbial Technology, v. 120, p. 16-22, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2018.09.009. Acesso em: 01 nov. 2024.
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      Monclaro, A. V., Recalde, G. L., Silva, F. G. da, Freitas, S. M. de, & Ferreira Filho, E. X. (2019). Xylanase from Aspergillus tamarii shows different kinetic parameters and substrate specificity in the presence of ferulic acid. Enzyme and Microbial Technology, 120, 16-22. doi:10.1016/j.enzmictec.2018.09.009
    • NLM

      Monclaro AV, Recalde GL, Silva FG da, Freitas SM de, Ferreira Filho EX. Xylanase from Aspergillus tamarii shows different kinetic parameters and substrate specificity in the presence of ferulic acid [Internet]. Enzyme and Microbial Technology. 2019 ; 120 16-22.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.009
    • Vancouver

      Monclaro AV, Recalde GL, Silva FG da, Freitas SM de, Ferreira Filho EX. Xylanase from Aspergillus tamarii shows different kinetic parameters and substrate specificity in the presence of ferulic acid [Internet]. Enzyme and Microbial Technology. 2019 ; 120 16-22.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.009
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: ENZIMAS, HIDRÓLISE, XANTHOMONAS

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      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: 01 nov. 2024.
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      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 2024 nov. 01 ] 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 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.05.007
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS

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      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: 01 nov. 2024.
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      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 nov. 01 ] 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 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
  • Source: Enzyme and Microbial Technology. Unidades: FCFRP, FFCLRP

    Subjects: ESPECTROMETRIA, ÁCIDOS, INFLAMAÇÃO, CROMATOGRAFIA LÍQUIDA

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      PETTA, Tânia et al. Inhibition of inflammatory response in LPS induced macrophages by 9-KOTE and 13-KOTE produced by biotransformation. Enzyme and Microbial Technology, v. 58-59, p. 36–43, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2014.02.011. Acesso em: 01 nov. 2024.
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      Petta, T., Secatto, A., Faccioli, L. H., & Moraes, L. A. B. de. (2014). Inhibition of inflammatory response in LPS induced macrophages by 9-KOTE and 13-KOTE produced by biotransformation. Enzyme and Microbial Technology, 58-59, 36–43. doi:10.1016/j.enzmictec.2014.02.011
    • NLM

      Petta T, Secatto A, Faccioli LH, Moraes LAB de. Inhibition of inflammatory response in LPS induced macrophages by 9-KOTE and 13-KOTE produced by biotransformation [Internet]. Enzyme and Microbial Technology. 2014 ; 58-59 36–43.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2014.02.011
    • Vancouver

      Petta T, Secatto A, Faccioli LH, Moraes LAB de. Inhibition of inflammatory response in LPS induced macrophages by 9-KOTE and 13-KOTE produced by biotransformation [Internet]. Enzyme and Microbial Technology. 2014 ; 58-59 36–43.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2014.02.011
  • Source: Enzyme and Microbial Technology. Unidade: IQSC

    Subjects: CÉLULAS A COMBUSTÍVEL, CATÁLISE

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      LA ROTTA HERNANDES, Camilo E. e CINICIATO, Gustavo Pio Marchesi Krall e GONZALEZ, Ernesto Rafael. Triphenylmethane dyes, an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells. Enzyme and Microbial Technology, v. 48, n. 6-7, p. 487-497, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2011.02.003. Acesso em: 01 nov. 2024.
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      La Rotta Hernandes, C. E., Ciniciato, G. P. M. K., & Gonzalez, E. R. (2011). Triphenylmethane dyes, an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells. Enzyme and Microbial Technology, 48( 6-7), 487-497. doi:10.1016/j.enzmictec.2011.02.003
    • NLM

      La Rotta Hernandes CE, Ciniciato GPMK, Gonzalez ER. Triphenylmethane dyes, an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells [Internet]. Enzyme and Microbial Technology. 2011 ; 48( 6-7): 487-497.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2011.02.003
    • Vancouver

      La Rotta Hernandes CE, Ciniciato GPMK, Gonzalez ER. Triphenylmethane dyes, an alternative for mediated electronic transfer systems in glucose oxidase biofuel cells [Internet]. Enzyme and Microbial Technology. 2011 ; 48( 6-7): 487-497.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2011.02.003
  • Source: Enzyme and Microbial Technology. Unidade: FCF

    Subjects: STREPTOMYCES, FERMENTAÇÃO

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      MARQUES, Daniela de Araújo Viana et al. Kinetic and thermodynamic investigation on clavulanic acid formation and degradation during glycerol fermentation by Streptomyces DAUFPE 3060. Enzyme and Microbial Technology, v. 45, n. 2, p. 169-173, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2009.03.005. Acesso em: 01 nov. 2024.
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      Marques, D. de A. V., Oliveira, R. P. de S., Perego, P., Porto, A. L. F., Pessoa Junior, A., & Converti, A. (2009). Kinetic and thermodynamic investigation on clavulanic acid formation and degradation during glycerol fermentation by Streptomyces DAUFPE 3060. Enzyme and Microbial Technology, 45( 2), 169-173. doi:10.1016/j.enzmictec.2009.03.005
    • NLM

      Marques D de AV, Oliveira RP de S, Perego P, Porto ALF, Pessoa Junior A, Converti A. Kinetic and thermodynamic investigation on clavulanic acid formation and degradation during glycerol fermentation by Streptomyces DAUFPE 3060 [Internet]. Enzyme and Microbial Technology. 2009 ; 45( 2): 169-173.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2009.03.005
    • Vancouver

      Marques D de AV, Oliveira RP de S, Perego P, Porto ALF, Pessoa Junior A, Converti A. Kinetic and thermodynamic investigation on clavulanic acid formation and degradation during glycerol fermentation by Streptomyces DAUFPE 3060 [Internet]. Enzyme and Microbial Technology. 2009 ; 45( 2): 169-173.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2009.03.005
  • Source: Enzyme and Microbial Technology. Unidade: FCF

    Subjects: EXTRAÇÃO DE LÍQUIDOS, PROTEÍNAS

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      JOZALA, Angela Faustino et al. Liquid-liquid extraction of commercial and biosynthesized nisin by aqueous two-phase micellar systems. Enzyme and Microbial Technology, v. 42, n. 2, p. 107-112, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2007.08.005. Acesso em: 01 nov. 2024.
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      Jozala, A. F., Lopes, A. M., Mazzola, P. G., Magalhães, P. de O. e, Vessoni Penna, T. C., & Pessoa Junior, A. (2008). Liquid-liquid extraction of commercial and biosynthesized nisin by aqueous two-phase micellar systems. Enzyme and Microbial Technology, 42( 2), 107-112. doi:10.1016/j.enzmictec.2007.08.005
    • NLM

      Jozala AF, Lopes AM, Mazzola PG, Magalhães P de O e, Vessoni Penna TC, Pessoa Junior A. Liquid-liquid extraction of commercial and biosynthesized nisin by aqueous two-phase micellar systems [Internet]. Enzyme and Microbial Technology. 2008 ;42( 2): 107-112.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2007.08.005
    • Vancouver

      Jozala AF, Lopes AM, Mazzola PG, Magalhães P de O e, Vessoni Penna TC, Pessoa Junior A. Liquid-liquid extraction of commercial and biosynthesized nisin by aqueous two-phase micellar systems [Internet]. Enzyme and Microbial Technology. 2008 ;42( 2): 107-112.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2007.08.005
  • Source: Enzyme and Microbial Technology. Unidade: FCFRP

    Assunto: ENZIMOLOGIA

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      LEITE, Rodrigo Simões Ribeiro et al. Production and characteristics comparison of crude 'beta'-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes. Enzyme and Microbial Technology, v. 43, n. 6, p. 391-395, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2008.07.006. Acesso em: 01 nov. 2024.
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      Leite, R. S. R., Alves-Prado, H. F., Cabral, H., Pagnocca, F. C., Gomes, E., & Da Silva, R. (2008). Production and characteristics comparison of crude 'beta'-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes. Enzyme and Microbial Technology, 43( 6), 391-395. doi:10.1016/j.enzmictec.2008.07.006
    • NLM

      Leite RSR, Alves-Prado HF, Cabral H, Pagnocca FC, Gomes E, Da Silva R. Production and characteristics comparison of crude 'beta'-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes [Internet]. Enzyme and Microbial Technology. 2008 ; 43( 6): 391-395.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2008.07.006
    • Vancouver

      Leite RSR, Alves-Prado HF, Cabral H, Pagnocca FC, Gomes E, Da Silva R. Production and characteristics comparison of crude 'beta'-glucosidases produced by microorganisms Thermoascus aurantiacus e Aureobasidium pullulans in agricultural wastes [Internet]. Enzyme and Microbial Technology. 2008 ; 43( 6): 391-395.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2008.07.006
  • Source: Enzyme and Microbial Technology. Unidades: ICB, IQ, IQSC

    Subjects: BIOTRANSFORMAÇÃO, QUÍMICA ORGÂNICA

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      RAMINELLI, Cristiano et al. Biotransformations of Mannich bases and propiophenones by Brazilian microorganisms and enzymatic resolution of phenylpropanols by lipase from Candida antarctica (Novozym 435). Enzyme and Microbial Technology, v. 40, n. 2, p. 362-369, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2006.06.002. Acesso em: 01 nov. 2024.
    • APA

      Raminelli, C., Kagohara, E., Pellizari, V. H., Comasseto, J. V., Andrade, L. H., & Porto, A. L. M. (2007). Biotransformations of Mannich bases and propiophenones by Brazilian microorganisms and enzymatic resolution of phenylpropanols by lipase from Candida antarctica (Novozym 435). Enzyme and Microbial Technology, 40( 2), 362-369. doi:10.1016/j.enzmictec.2006.06.002
    • NLM

      Raminelli C, Kagohara E, Pellizari VH, Comasseto JV, Andrade LH, Porto ALM. Biotransformations of Mannich bases and propiophenones by Brazilian microorganisms and enzymatic resolution of phenylpropanols by lipase from Candida antarctica (Novozym 435) [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 2): 362-369.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.06.002
    • Vancouver

      Raminelli C, Kagohara E, Pellizari VH, Comasseto JV, Andrade LH, Porto ALM. Biotransformations of Mannich bases and propiophenones by Brazilian microorganisms and enzymatic resolution of phenylpropanols by lipase from Candida antarctica (Novozym 435) [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 2): 362-369.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.06.002
  • Source: Enzyme and Microbial Technology. Unidade: FCF

    Subjects: TERMODINÂMICA, SACCHAROMYCES, EXTRAÇÃO DE LÍQUIDOS

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    • ABNT

      HASMANN, Francislene Andréia et al. New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability. Enzyme and Microbial Technology, v. 40, n. 4, p. 849-858, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2006.06.017. Acesso em: 01 nov. 2024.
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      Hasmann, F. A., Gurpilhares, D. de B., Roberto, I. C., Converti, A., & Pessoa Junior, A. (2007). New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability. Enzyme and Microbial Technology, 40( 4), 849-858. doi:10.1016/j.enzmictec.2006.06.017
    • NLM

      Hasmann FA, Gurpilhares D de B, Roberto IC, Converti A, Pessoa Junior A. New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 4): 849-858.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.06.017
    • Vancouver

      Hasmann FA, Gurpilhares D de B, Roberto IC, Converti A, Pessoa Junior A. New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 4): 849-858.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.06.017
  • Source: Enzyme and Microbial Technology. Unidade: FCF

    Subjects: OXIDAÇÃO, FERMENTAÇÃO, ENZIMAS

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      TOMOTANI, Ester Junko e VITOLO, Michele. Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor. Enzyme and Microbial Technology, v. 40, n. 5, p. 1020-1025, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2006.07.039. Acesso em: 01 nov. 2024.
    • APA

      Tomotani, E. J., & Vitolo, M. (2007). Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor. Enzyme and Microbial Technology, 40( 5), 1020-1025. doi:10.1016/j.enzmictec.2006.07.039
    • NLM

      Tomotani EJ, Vitolo M. Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 5): 1020-1025.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.07.039
    • Vancouver

      Tomotani EJ, Vitolo M. Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 5): 1020-1025.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.07.039

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