In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol (2011)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: DIGESTÃO ANIMAL; ENZIMAS
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq)
- Publisher place: São Paulo
- Date published: 2011
- Source:
- Título: Program and Index
- Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society (SBBq)
-
ABNT
ROZENBERGT, Roberto e MARANA, Sandro Roberto. In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol. 2011, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2011. . Acesso em: 29 dez. 2025. -
APA
Rozenbergt, R., & Marana, S. R. (2011). In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq). -
NLM
Rozenbergt R, Marana SR. In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol. Program and Index. 2011 ;[citado 2025 dez. 29 ] -
Vancouver
Rozenbergt R, Marana SR. In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol. Program and Index. 2011 ;[citado 2025 dez. 29 ] - Optimum temperature may be a misleading parameter in enzyme characterization and application
- Enzyme optimum temperature: constant or relative parameter?
- Role of the triad N46, S106 and T107 and the surface charges in the determination of the acidic pH optimum of digestive lysozymes from Musca domestica
- Additivity of mutational effects on the catalytic activity of a 'beta'glycosidase
- Role of residue E190 in modulating aglycone specificity of a 'beta'-glycosidase from spodoptera frugiperda (SFBGLI50-AF 052729) of family 1
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
- Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase
- Standardization of a method of In vitro evolution of beta-glycosidases
- The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase
- Study of the molecular basis for the substrate specificity in a `beta´-glycosidase by using directed evolution
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