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Mode of action, kinetic properties and physicochemical characterization of two different domains of a bifunctional (1-->4)-beta-D-xylanase from Ruminococcus flavefaciens expressed separately in Escherichia coli.

Two catalytic domains, A and C, of xylanase A (XYLA) from Ruminococcus flavefaciens were expressed separately as truncated gene products from lacZ fusions in Escherichia coli. The fusion products, referred to respectively as XYLA-A1 and XYLA-C2, were purified to homogeneity by anion-exchange chromat...

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Detalhes bibliográficos
Main Authors: Garcia-Campayo, V, McCrae, S I, Zhang, J X, Flint, H J, Wood, T M
Formato: Artigo
Idioma:Inglês
Publicado em: 1993
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1137679/
https://ncbi.nlm.nih.gov/pubmed/8250849
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