Data/hora: 04/06/2024 12:39:32

Provedor de dados: 	58	
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	
Fonte: 	info:eu-repo/semantics/openAccess