Recombinant Expression and Characterization of a Reducing-End Xylose-Releasing Exo-Oligoxylanase from Bifidobacterium adolescentis

• Published in: Applied and Environmental Microbiology Vol. 73; no. 16; pp. 5374 - 5377
• Main Authors: Lagaert, Stijn, Van Campenhout, Steven, Pollet, Annick, Bourgois, Tine M, Delcour, Jan A, Courtin, Christophe M, Volckaert, Guido
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.08.2007
• Subjects: Amino Acid Sequence; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bifidobacterium - enzymology; Bifidobacterium - genetics; Bifidobacterium - metabolism; Bifidobacterium adolescentis; Biological and medical sciences; E coli; Electrophoresis, Polyacrylamide Gel; enzyme activity; Enzymes; Enzymology and Protein Engineering; Escherichia coli; Fundamental and applied biological sciences. Psychology; Gene expression; gene transfer; Glycoside Hydrolases - genetics; Glycoside Hydrolases - metabolism; Hydrogen-Ion Concentration; Hydrolysis; Microbiology; Molecular Sequence Data; Phylogeny; recombinant proteins; Recombinant Proteins - metabolism; Sequence Homology, Amino Acid; Temperature; xylanases; xylooligosaccharides; Xylose - metabolism; Actinomycetales; Characterization; Xylose; Lactic acid bacteria; Actinomycetaceae; Bifidobacterium adolescentis; Bacteria; Actinomycetes
• ISSN: 0099-2240; 1098-5336
• DOI: 10.1128/AEM.00722-07

The family 8 glycoside hydrolase (RexA) from Bifidobacterium adolescentis was expressed in Escherichia coli. The recombinant enzyme was characterized as a reducing-end xylose-releasing exo-oligoxylanase. Apart from giving insights into this new class of enzymes, knowledge of the RexA enzyme helps to postulate a mechanism for the B. adolescentis breakdown of prebiotic xylooligosaccharides.