Construction, recombinant expression and characterization of site-directed mutants of a digestive lysozyme (2009)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: LISOZIMAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq
- Publisher place: São Paulo
- Date published: 2009
- Source:
- Título do periódico: Program and Index
- Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society
-
ABNT
HENRIQUES, Nadia Michtchenko e MARANA, Sandro Roberto. Construction, recombinant expression and characterization of site-directed mutants of a digestive lysozyme. 2009, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2009. . Acesso em: 25 set. 2024. -
APA
Henriques, N. M., & Marana, S. R. (2009). Construction, recombinant expression and characterization of site-directed mutants of a digestive lysozyme. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. -
NLM
Henriques NM, Marana SR. Construction, recombinant expression and characterization of site-directed mutants of a digestive lysozyme. Program and Index. 2009 ;[citado 2024 set. 25 ] -
Vancouver
Henriques NM, Marana SR. Construction, recombinant expression and characterization of site-directed mutants of a digestive lysozyme. Program and Index. 2009 ;[citado 2024 set. 25 ] - 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
- In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol
- 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
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