Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities (2017)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: ENZIMOLOGIA; GLICOSÍDEOS
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq
- Publisher place: São Paulo
- Date published: 2017
- Source:
- Título: Abstracts
- Conference titles: 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: 10 jan. 2026. -
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 2026 jan. 10 ] -
Vancouver
Almeida VM, Marana SR. Identification of domains in GH1 β-glucosidases based on the thermal and chemical stabilities. Abstracts. 2017 ;[citado 2026 jan. 10 ] - Effects upon the stability of Sfbglu caused by mutations surrounding central residues
- The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase
- Single mutations outside the active site affect the substrate specificity in a ß-glycosidade
- Standardization of a method of In vitro evolution of beta-glycosidases
- Determinação do calor de reação para peroxiredoxinas
- Distribuicao intracelular de enzimas digestivas e caracterizacao das 'BETA'-glucosidases intestinais de abracris flavolineata
- Mutation of surface charged residues changes the affinity of lysozymes for bacterial walls
- 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
- Enzyme optimum temperature: constant or relative parameter?
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
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