Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from Thermoascus aurantiacus.

An extracellular beta-glucosidase from Thermoascus aurantiacus was purified to homogeneity by DEAE-Sepharose, Ultrogel AcA 44 and Mono-P column chromatography. The enzyme was a homotrimer, with a monomer molecular mass of 120 kDa; only the trimer was optimally active at 80 degrees C and at pH 4.5. A...

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Autores principales: Parry, N J, Beever, D E, Owen, E, Vandenberghe, I, Van Beeumen , J, Bhat, M K
Formato: Artigo
Lenguaje:Inglês
Publicado: 2001
Materias:
Research Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1221549/
https://ncbi.nlm.nih.gov/pubmed/11115405
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