| Registro completo |
| Provedor de dados: |
BJM
|
| País: |
Brazil
|
| Título: |
Chemical modification of Aspergillus nigerβ-glucosidase and its catalytic properties
|
| Autores: |
Ahmed,Samia A.
El-Shayeb,Nefisa M.A.
Hashem,Abdel-Gawad M.
Saleh,Shireen A.A.
Abdel-Fattah,Ahmed F.
|
| Data: |
2015-03-01
|
| Ano: |
2015
|
| Palavras-chave: |
Β-glucosidases
Glycosylation
Soluble polysaccharides
Enzyme stability
|
| Resumo: |
Aspergillus niger β-glucosidase was modified by covalent coupling to periodate activated polysaccharides (glycosylation). The conjugated enzyme to activated starch showed the highest specific activity (128.5 U/mg protein). Compared to the native enzyme, the conjugated form exhibited: a higher optimal reaction temperature, a lower Ea (activation energy), a higher Km (Michaelis constant) and Vmax (maximal reaction rate), and improved thermal stability. The calculated t1/2 (half-life) values of heat in-activation at 60 °C and 70 °C were 245.7 and 54.5 min respectively, whereas at these temperatures the native enzyme was less stable (t1/2of 200.0 and 49.5 min respectively). The conjugated enzyme retained 32.3 and 29.7%, respectively from its initial activity in presence of 5 mM Sodium Dodecyl Sulphate (SDS) and p-Chloro Mercuri Benzoate (p-CMB), while the native enzyme showed a remarkable loss of activity (retained activity 1.61 and 13.7%, respectively). The present work has established the potential of glycosylation to enhance the catalytic properties of β-glucosidase enzyme, making this enzyme potentially feasible for biotechnological applications.
|
| Tipo: |
Info:eu-repo/semantics/article
|
| Idioma: |
Inglês
|
| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000100023
|
| Editor: |
Sociedade Brasileira de Microbiologia
|
| Relação: |
10.1590/S1517-838246120120462
|
| Formato: |
text/html
|
| Fonte: |
Brazilian Journal of Microbiology v.46 n.1 2015
|
| Direitos: |
info:eu-repo/semantics/openAccess
|
