Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities (2017)
- Authors:
- USP affiliated author: MARANA, SANDRO ROBERTO - IQ
- School: IQ
- Subjects: ENZIMOLOGIA; GLICOSÍDEOS
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq
- Place of publication: São Paulo
- Date published: 2017
- Source:
- Título do periódico: Abstracts
- Conference title: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology
-
ABNT
ALMEIDA, Vitor Medeiros e MARANA, Sandro Roberto. Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities. 2017, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq, 2017. . Acesso em: 29 jun. 2022. -
APA
Almeida, V. M., & Marana, S. R. (2017). Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq. -
NLM
Almeida VM, Marana SR. Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities. Abstracts. 2017 ;[citado 2022 jun. 29 ] -
Vancouver
Almeida VM, Marana SR. Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities. Abstracts. 2017 ;[citado 2022 jun. 29 ] - Standardization of a method of In vitro evolution of beta-glycosidases
- 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
- Study of the molecular basis for the substrate specificity in a `beta´-glycosidase by using directed evolution
- 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
- In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol
- Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
- Enzyme optimum temperature: constant or relative parameter?
- Protein structure network and thermal stability
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