A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis (2016)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.1016/j.bbrep.2016.05.014
- Subjects: HIDRÓLISE; CELULOSE; ENZIMAS
- Language: Inglês
- Imprenta:
- Publisher place: Philadelphia
- Date published: 2016
- Source:
- Título do periódico: Biochemistry and Biophysics Reports
- ISSN: 2405-5808
- Volume/Número/Paginação/Ano: v. 7, p. 52-55, 2016
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by-nc-nd
-
ABNT
TAMAKI, Fabio Kendi et al. A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis. Biochemistry and Biophysics Reports, v. 7, p. 52-55, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.bbrep.2016.05.014. Acesso em: 23 abr. 2024. -
APA
Tamaki, F. K., Araujo, É. M., Rozenberg, R., & Marana, S. R. (2016). A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis. Biochemistry and Biophysics Reports, 7, 52-55. doi:10.1016/j.bbrep.2016.05.014 -
NLM
Tamaki FK, Araujo ÉM, Rozenberg R, Marana SR. A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis [Internet]. Biochemistry and Biophysics Reports. 2016 ; 7 52-55.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.bbrep.2016.05.014 -
Vancouver
Tamaki FK, Araujo ÉM, Rozenberg R, Marana SR. A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis [Internet]. Biochemistry and Biophysics Reports. 2016 ; 7 52-55.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.bbrep.2016.05.014 - 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
Informações sobre o DOI: 10.1016/j.bbrep.2016.05.014 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas