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.

Garcia-Campayo, V

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. [electronic resource] - The Biochemical journal Nov 1993 - 235-43 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

0264-6021

10.1042/bj2960235 doi


Animals
Bacteria, Anaerobic--enzymology
Binding Sites
Carbohydrate Sequence
Chromatography, Ion Exchange
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Endo-1,4-beta Xylanases
Escherichia coli
Gene Expression
Genes, Bacterial
Glycoside Hydrolases--biosynthesis
Gram-Positive Cocci--enzymology
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Molecular Weight
Oligosaccharides--metabolism
Recombinant Proteins--biosynthesis
Rumen--microbiology