Expression of Two Novel ß-Glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and Characterization of the Heterologous Protein Products.
Mol Biotechnol
; 58(12): 821-831, 2016 Dec.
Article
em En
| MEDLINE
| ID: mdl-27714589
ABSTRACT
Two novel GH3 family thermostable ß-glucosidases from the filamentous fungus Chaetomium atrobrunneum (CEL3a and CEL3b) were expressed in Trichoderma reesei, purified by two-step ion exchange chromatography, and characterized. Both enzymes were active over a wide range of pH as compared to Neurospora crassa ß-glucosidase GH3-3, which was also expressed in T. reesei and purified. The optimum temperature of both C. atrobrunneum enzymes was around 60 °C at pH 5, and both enzymes had better thermal and pH stability and higher resistance to metallic compounds and to glucose inhibition than GH3-3. They also showed higher activity against oligosaccharides composed of glucose units and linked with ß-1,4-glycosidic bonds and moreover, had higher affinity for cellotriose over cellobiose. In hydrolysis tests against Avicel cellulose and steam-exploded sugarcane bagasse, performed at 45 °C, particularly the CEL3a enzyme performed similarly to N. crassa GH3-3 ß-glucosidase. Taking into account the thermal stability of the C. atrobrunneum ß-glucosidases, they both represent promising alternatives as enzyme mixture components for improved cellulose saccharification at elevated temperatures.
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Base de dados:
MEDLINE
Assunto principal:
Trichoderma
/
Chaetomium
/
Beta-Glucosidase
Idioma:
En
Revista:
Mol Biotechnol
Assunto da revista:
BIOLOGIA MOLECULAR
/
BIOTECNOLOGIA
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Finlândia