Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans (2016)
- Authors:
- USP affiliated authors: SANTOS, MARIA AUXILIADORA MORIM - IFSC ; MARANA, SANDRO ROBERTO - IQ ; POLIKARPOV, IGOR - IFSC
- Unidades: IFSC; IQ
- DOI: 10.1007/s12033-016-9977-3
- Subjects: MODELAGEM MOLECULAR; GLICOSÍDEOS
- Keywords: Glycosidase hydrolase family 1; Saccharophagus degradans; Enzymatic characterization; Modelling; SAXS structure
- Language: Inglês
- Imprenta:
- Source:
- Título: Molecular Biotechnology
- ISSN: 1073-6085
- Volume/Número/Paginação/Ano: v. 58, n. 12, p. 777-788, Dec. 2016
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
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ABNT
BROGNARO, Hevila et al. Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans. Molecular Biotechnology, v. 58, n. 12, p. 777-788, 2016Tradução . . Disponível em: https://doi.org/10.1007/s12033-016-9977-3. Acesso em: 03 out. 2024. -
APA
Brognaro, H., Almeida, V. M., Araújo, E. A. de, Piyadov, V., Santos, M. A. M., Marana, S. R., & Polikarpov, I. (2016). Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans. Molecular Biotechnology, 58( 12), 777-788. doi:10.1007/s12033-016-9977-3 -
NLM
Brognaro H, Almeida VM, Araújo EA de, Piyadov V, Santos MAM, Marana SR, Polikarpov I. Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans [Internet]. Molecular Biotechnology. 2016 ; 58( 12): 777-788.[citado 2024 out. 03 ] Available from: https://doi.org/10.1007/s12033-016-9977-3 -
Vancouver
Brognaro H, Almeida VM, Araújo EA de, Piyadov V, Santos MAM, Marana SR, Polikarpov I. Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans [Internet]. Molecular Biotechnology. 2016 ; 58( 12): 777-788.[citado 2024 out. 03 ] Available from: https://doi.org/10.1007/s12033-016-9977-3 - Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability
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- Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda
- Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase
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- Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis
- Optimum temperature may be a misleading parameter in enzyme characterization and application
- Enzyme optimum temperature: constant or relative parameter?
Informações sobre o DOI: 10.1007/s12033-016-9977-3 (Fonte: oaDOI API)
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