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Artigo de periodico
Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase (2021)
Araújo, Evandro Ares de; Dias, Artur Hermano Sampaio; Kadowaki, Marco Antonio Seiki ; Piyadov, Vasily; Pellegrini, Vanessa de Oliveira Arnoldi ; Urio, Mateus B.; Ramos, Luiz P.; Skaf, Munir S.; Polikarpov, Igor
Source: Carbohydrate Polymers. Unidade: IFSC
Subjects: CELULOSE, BAGAÇOS, CANA-DE-AÇÚCAR, MATERIAIS NANOESTRUTURADOS, ENZIMAS
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ABNT
ARAÚJO, Evandro Ares de et al. Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase. Carbohydrate Polymers, v. 264, p. 118059-1-118059-13, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.carbpol.2021.118059. Acesso em: 14 out. 2024.
APA
Araújo, E. A. de, Dias, A. H. S., Kadowaki, M. A. S., Piyadov, V., Pellegrini, V. de O. A., Urio, M. B., et al. (2021). Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase. Carbohydrate Polymers, 264, 118059-1-118059-13. doi:10.1016/j.carbpol.2021.118059
NLM
Araújo EA de, Dias AHS, Kadowaki MAS, Piyadov V, Pellegrini V de OA, Urio MB, Ramos LP, Skaf MS, Polikarpov I. Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase [Internet]. Carbohydrate Polymers. 2021 ; 264 118059-1-118059-13.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.carbpol.2021.118059
Vancouver
Araújo EA de, Dias AHS, Kadowaki MAS, Piyadov V, Pellegrini V de OA, Urio MB, Ramos LP, Skaf MS, Polikarpov I. Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase [Internet]. Carbohydrate Polymers. 2021 ; 264 118059-1-118059-13.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.carbpol.2021.118059
Artigo de periodico
Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium (2021)
Kadowaki, Marco Antonio Seiki ; Briganti, Lorenzo ; Evangelista, Danilo Elton ; Echevarría-Poza, Alberto; Tryfona, Theodora ; Pellegrini, Vanessa de Oliveira Arnoldi ; Nakayama, Darlan Gonçalves ; Dupree, Paul ; Polikarpov, Igor
Source: Biotechnology and Bioengineering. Unidade: IFSC
Subjects: BIOMASSA, HETEROPOLISSACARÍDEOS, PAREDE CELULAR VEGETAL
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ABNT
KADOWAKI, Marco Antonio Seiki et al. Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium. Biotechnology and Bioengineering, v. 118, n. 10, p. 4052-4064, 2021Tradução . . Disponível em: https://doi.org/10.1002/bit.27880. Acesso em: 14 out. 2024.
APA
Kadowaki, M. A. S., Briganti, L., Evangelista, D. E., Echevarría-Poza, A., Tryfona, T., Pellegrini, V. de O. A., et al. (2021). Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium. Biotechnology and Bioengineering, 118( 10), 4052-4064. doi:10.1002/bit.27880
NLM
Kadowaki MAS, Briganti L, Evangelista DE, Echevarría-Poza A, Tryfona T, Pellegrini V de OA, Nakayama DG, Dupree P, Polikarpov I. Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium [Internet]. Biotechnology and Bioengineering. 2021 ; 118( 10): 4052-4064.[citado 2024 out. 14 ] Available from: https://doi.org/10.1002/bit.27880
Vancouver
Kadowaki MAS, Briganti L, Evangelista DE, Echevarría-Poza A, Tryfona T, Pellegrini V de OA, Nakayama DG, Dupree P, Polikarpov I. Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium [Internet]. Biotechnology and Bioengineering. 2021 ; 118( 10): 4052-4064.[citado 2024 out. 14 ] Available from: https://doi.org/10.1002/bit.27880
Artigo de periodico
Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris (2020)
Velasco, Josman ; Oliva, Bianca ; Gonçalves, Aline Larissa; Lima, Awana Silva ; Ferreira, Gislene; França, Bruno Alves; Mulinari, Evandro José ; Gonçalves, Thiago Augusto ; Squina, Fábio Márcio ; Kadowaki, Marco Antonio Seiki ; Maiorano, Alfredo ; Polikarpov, Igor ; Oliveira, Leandro Cristante de ; Segato, Fernando
Source: Applied Microbiology and Biotechnology. Unidades: IFSC, EEL
Subjects: ASPERGILLUS, BETERRABA AÇUCAREIRA, FUNGOS TERMÓFILOS
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ABNT
VELASCO, Josman et al. Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris. Applied Microbiology and Biotechnology, v. 104, n. 19, p. 8309-8326, 2020Tradução . . Disponível em: https://doi.org/10.1007/s00253-020-10806-6. Acesso em: 14 out. 2024.
APA
Velasco, J., Oliva, B., Gonçalves, A. L., Lima, A. S., Ferreira, G., França, B. A., et al. (2020). Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris. Applied Microbiology and Biotechnology, 104( 19), 8309-8326. doi:10.1007/s00253-020-10806-6
NLM
Velasco J, Oliva B, Gonçalves AL, Lima AS, Ferreira G, França BA, Mulinari EJ, Gonçalves TA, Squina FM, Kadowaki MAS, Maiorano A, Polikarpov I, Oliveira LC de, Segato F. Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris [Internet]. Applied Microbiology and Biotechnology. 2020 ; 104( 19): 8309-8326.[citado 2024 out. 14 ] Available from: https://doi.org/10.1007/s00253-020-10806-6
Vancouver
Velasco J, Oliva B, Gonçalves AL, Lima AS, Ferreira G, França BA, Mulinari EJ, Gonçalves TA, Squina FM, Kadowaki MAS, Maiorano A, Polikarpov I, Oliveira LC de, Segato F. Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris [Internet]. Applied Microbiology and Biotechnology. 2020 ; 104( 19): 8309-8326.[citado 2024 out. 14 ] Available from: https://doi.org/10.1007/s00253-020-10806-6
Artigo de periodico
Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77 (2020)
Kadowaki, Marco Antonio Seiki; Higasi, Paula Miwa Rabêlo ; Godoy, Mariana Ortiz de; Araújo, Evandro Ares de; Godoy, Andre Schutzer de ; Prade, Rolf Alexander; Polikarpov, Igor
Source: Biochimica et Biophysica Acta: general subjects. Unidade: IFSC
Subjects: FUNGOS TERMÓFILOS, ENZIMAS, ÁLCOOL, BIOTECNOLOGIA
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ABNT
KADOWAKI, Marco Antonio Seiki et al. Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77. Biochimica et Biophysica Acta: general subjects, v. 1864, n. 10, p. 129681-1-129681-13, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bbagen.2020.129681. Acesso em: 14 out. 2024.
APA
Kadowaki, M. A. S., Higasi, P. M. R., Godoy, M. O. de, Araújo, E. A. de, Godoy, A. S. de, Prade, R. A., & Polikarpov, I. (2020). Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77. Biochimica et Biophysica Acta: general subjects, 1864( 10), 129681-1-129681-13. doi:10.1016/j.bbagen.2020.129681
NLM
Kadowaki MAS, Higasi PMR, Godoy MO de, Araújo EA de, Godoy AS de, Prade RA, Polikarpov I. Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77 [Internet]. Biochimica et Biophysica Acta: general subjects. 2020 ; 1864( 10): 129681-1-129681-13.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.bbagen.2020.129681
Vancouver
Kadowaki MAS, Higasi PMR, Godoy MO de, Araújo EA de, Godoy AS de, Prade RA, Polikarpov I. Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77 [Internet]. Biochimica et Biophysica Acta: general subjects. 2020 ; 1864( 10): 129681-1-129681-13.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.bbagen.2020.129681
Artigo de periodico
Multienzyme cellulose films as sustainable and self-degradable hydrogen peroxide-producing material (2020)
Califano, Davide; Kadowaki, Marco Antonio Seiki ; Calabrese, Vincenzo; Prade, Rolf Alexander; Mattia, Davide ; Edler, Karen J. ; Polikarpov, Igor ; Scott, Janet L.
Source: Biomacromolecules. Unidade: IFSC
Subjects: FILMES FINOS, BIOMATERIAIS, CELULOSE, BIOTECNOLOGIA
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ABNT
CALIFANO, Davide et al. Multienzyme cellulose films as sustainable and self-degradable hydrogen peroxide-producing material. Biomacromolecules, v. 21, n. 12, p. 5315-5322, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.biomac.0c01393. Acesso em: 14 out. 2024.
APA
Califano, D., Kadowaki, M. A. S., Calabrese, V., Prade, R. A., Mattia, D., Edler, K. J., et al. (2020). Multienzyme cellulose films as sustainable and self-degradable hydrogen peroxide-producing material. Biomacromolecules, 21( 12), 5315-5322. doi:10.1021/acs.biomac.0c01393
NLM
Califano D, Kadowaki MAS, Calabrese V, Prade RA, Mattia D, Edler KJ, Polikarpov I, Scott JL. Multienzyme cellulose films as sustainable and self-degradable hydrogen peroxide-producing material [Internet]. Biomacromolecules. 2020 ; 21( 12): 5315-5322.[citado 2024 out. 14 ] Available from: https://doi.org/10.1021/acs.biomac.0c01393
Vancouver
Califano D, Kadowaki MAS, Calabrese V, Prade RA, Mattia D, Edler KJ, Polikarpov I, Scott JL. Multienzyme cellulose films as sustainable and self-degradable hydrogen peroxide-producing material [Internet]. Biomacromolecules. 2020 ; 21( 12): 5315-5322.[citado 2024 out. 14 ] Available from: https://doi.org/10.1021/acs.biomac.0c01393
Artigo de periodico
Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A (2019)
Kadowaki, Marco Antonio Seiki; Polikarpov, Igor
Source: Biochimie. Unidade: IFSC
Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE
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ABNT
KADOWAKI, Marco Antonio Seiki e POLIKARPOV, Igor. Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A. Biochimie, v. 165, p. 275-284, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2019.08.016. Acesso em: 14 out. 2024.
APA
Kadowaki, M. A. S., & Polikarpov, I. (2019). Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A. Biochimie, 165, 275-284. doi:10.1016/j.biochi.2019.08.016
NLM
Kadowaki MAS, Polikarpov I. Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A [Internet]. Biochimie. 2019 ; 165 275-284.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.biochi.2019.08.016
Vancouver
Kadowaki MAS, Polikarpov I. Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A [Internet]. Biochimie. 2019 ; 165 275-284.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.biochi.2019.08.016
Artigo de periodico
Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia (2018)
Evangelista, Danilo Elton; Kadowaki, Marco Antonio Seiki; Mello, Bruno Luan; Polikarpov, Igor
Source: International Journal of Biological Macromolecules. Unidade: IFSC
Subjects: ENZIMAS, BIOTECNOLOGIA, BAGAÇOS, CANA-DE-AÇÚCAR
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ABNT
EVANGELISTA, Danilo Elton et al. Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia. International Journal of Biological Macromolecules, v. 109, p. 560-568, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.12.099. Acesso em: 14 out. 2024.
APA
Evangelista, D. E., Kadowaki, M. A. S., Mello, B. L., & Polikarpov, I. (2018). Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia. International Journal of Biological Macromolecules, 109, 560-568. doi:10.1016/j.ijbiomac.2017.12.099
NLM
Evangelista DE, Kadowaki MAS, Mello BL, Polikarpov I. Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia [Internet]. International Journal of Biological Macromolecules. 2018 ; 109 560-568.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.099
Vancouver
Evangelista DE, Kadowaki MAS, Mello BL, Polikarpov I. Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia [Internet]. International Journal of Biological Macromolecules. 2018 ; 109 560-568.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.099
Artigo de periodico
Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis (2018)
Araújo, Evandro Ares de; Manzine, Livia Regina; Piiadov, Vassili; Kadowaki, Marco Antonio Seiki; Polikarpov, Igor
Source: International Journal of Biological Macromolecules. Unidade: IFSC
Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE
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ABNT
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: 14 out. 2024.
APA
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
NLM
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 2024 out. 14 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.138
Vancouver
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 2024 out. 14 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.138
Artigo de periodico
Biochemical characterization and low-resolution SAXS structure of an exopolygalacturonase from Bacillus licheniformis (2018)
Evangelista, Danilo Elton; Araújo, Evandro A.; Oliveira Neto, Mario de; Kadowaki, Marco Antonio Seiki; Polikarpov, Igor
Source: New Biotechnology. Unidade: IFSC
Subjects: TRICHODERMA, ENZIMAS
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ABNT
EVANGELISTA, Danilo Elton et al. Biochemical characterization and low-resolution SAXS structure of an exopolygalacturonase from Bacillus licheniformis. New Biotechnology, v. 40, n. Ja 2018, p. 268-274, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.nbt.2017.10.001. Acesso em: 14 out. 2024.
APA
Evangelista, D. E., Araújo, E. A., Oliveira Neto, M. de, Kadowaki, M. A. S., & Polikarpov, I. (2018). Biochemical characterization and low-resolution SAXS structure of an exopolygalacturonase from Bacillus licheniformis. New Biotechnology, 40( Ja 2018), 268-274. doi:10.1016/j.nbt.2017.10.001
NLM
Evangelista DE, Araújo EA, Oliveira Neto M de, Kadowaki MAS, Polikarpov I. Biochemical characterization and low-resolution SAXS structure of an exopolygalacturonase from Bacillus licheniformis [Internet]. New Biotechnology. 2018 ; 40( Ja 2018): 268-274.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.nbt.2017.10.001
Vancouver
Evangelista DE, Araújo EA, Oliveira Neto M de, Kadowaki MAS, Polikarpov I. Biochemical characterization and low-resolution SAXS structure of an exopolygalacturonase from Bacillus licheniformis [Internet]. New Biotechnology. 2018 ; 40( Ja 2018): 268-274.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.nbt.2017.10.001
Artigo de periodico
Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis (2018)
Nakamura, Aline M.; Kadowaki, Marco Antonio Seiki; Godoy, André; Nascimento, Alessandro Silva ; Polikarpov, Igor
Source: International Journal of Biological Macromolecules. Unidade: IFSC
Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE
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ABNT
NAKAMURA, Aline M. et al. Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis. International Journal of Biological Macromolecules, v. 120, p. 1893-1905, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2018.10.003. Acesso em: 14 out. 2024.
APA
Nakamura, A. M., Kadowaki, M. A. S., Godoy, A., Nascimento, A. S., & Polikarpov, I. (2018). Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis. International Journal of Biological Macromolecules, 120, 1893-1905. doi:10.1016/j.ijbiomac.2018.10.003
NLM
Nakamura AM, Kadowaki MAS, Godoy A, Nascimento AS, Polikarpov I. Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis [Internet]. International Journal of Biological Macromolecules. 2018 ; 120 1893-1905.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.10.003
Vancouver
Nakamura AM, Kadowaki MAS, Godoy A, Nascimento AS, Polikarpov I. Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis [Internet]. International Journal of Biological Macromolecules. 2018 ; 120 1893-1905.[citado 2024 out. 14 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.10.003
Artigo de periodico
Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation (2018)
Kadowaki, Marco Antonio Seiki; Godoy, Mariana Ortiz de; Kumagai, Patricia Suemy; Costa Filho, Antonio José da; Mort, Andrew; Prade, Rolf Alexander; Polikarpov, Igor
Source: Catalysts. Unidades: FFCLRP, IFSC
Subjects: ENZIMAS, FUNGOS TERMÓFILOS, RESSONÂNCIA PARAMAGNÉTICA ELETRÔNICA
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ABNT
KADOWAKI, Marco Antonio Seiki et al. Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation. Catalysts, v. 8, n. 10, p. 476-1-476-15, 2018Tradução . . Disponível em: https://doi.org/10.3390/catal8100476. Acesso em: 14 out. 2024.
APA
Kadowaki, M. A. S., Godoy, M. O. de, Kumagai, P. S., Costa Filho, A. J. da, Mort, A., Prade, R. A., & Polikarpov, I. (2018). Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation. Catalysts, 8( 10), 476-1-476-15. doi:10.3390/catal8100476
NLM
Kadowaki MAS, Godoy MO de, Kumagai PS, Costa Filho AJ da, Mort A, Prade RA, Polikarpov I. Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation [Internet]. Catalysts. 2018 ; 8( 10): 476-1-476-15.[citado 2024 out. 14 ] Available from: https://doi.org/10.3390/catal8100476
Vancouver
Kadowaki MAS, Godoy MO de, Kumagai PS, Costa Filho AJ da, Mort A, Prade RA, Polikarpov I. Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation [Internet]. Catalysts. 2018 ; 8( 10): 476-1-476-15.[citado 2024 out. 14 ] Available from: https://doi.org/10.3390/catal8100476

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