Enzymatic oxidation chemistry linked to biomass degradation in Myceliophthora thermophile: biochemical and structural characterization of the oxidative enzymes glyoxal (Gox) and aryl-alcohol (GloA) oxidase (2015)
- Authors:
- Autor USP: POLIKARPOV, IGOR - IFSC
- Unidade: IFSC
- Subjects: ENZIMAS; BACTÉRIAS TERMÓFILAS; BIOMASSA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq
- Publisher place: São Paulo
- Date published: 2015
- Source:
- Título do periódico: Abstracts Book
- Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - IUBMB
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ABNT
KADOWAKI, M. A. S. et al. Enzymatic oxidation chemistry linked to biomass degradation in Myceliophthora thermophile: biochemical and structural characterization of the oxidative enzymes glyoxal (Gox) and aryl-alcohol (GloA) oxidase. 2015, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2015. . Acesso em: 17 abr. 2024. -
APA
Kadowaki, M. A. S., Godoy, M. O., Miotto, L. S., Polikarpov, I., & Prade, R. A. (2015). Enzymatic oxidation chemistry linked to biomass degradation in Myceliophthora thermophile: biochemical and structural characterization of the oxidative enzymes glyoxal (Gox) and aryl-alcohol (GloA) oxidase. In Abstracts Book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. -
NLM
Kadowaki MAS, Godoy MO, Miotto LS, Polikarpov I, Prade RA. Enzymatic oxidation chemistry linked to biomass degradation in Myceliophthora thermophile: biochemical and structural characterization of the oxidative enzymes glyoxal (Gox) and aryl-alcohol (GloA) oxidase. Abstracts Book. 2015 ;[citado 2024 abr. 17 ] -
Vancouver
Kadowaki MAS, Godoy MO, Miotto LS, Polikarpov I, Prade RA. Enzymatic oxidation chemistry linked to biomass degradation in Myceliophthora thermophile: biochemical and structural characterization of the oxidative enzymes glyoxal (Gox) and aryl-alcohol (GloA) oxidase. Abstracts Book. 2015 ;[citado 2024 abr. 17 ] - Estudos estruturais e funcionais de xilanases com potencial aplicação biotecnológica
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