Activity of an Aspergillus terreus alpha-arabinofuranosidase on phenolic-substituted oligosaccharides.
The effect of phenolic substitutions on the activity of an alpha-arabinofuranosidase from Aspergillus terreus was investigated using feruloylated oligosaccharides isolated from plant cell walls, equivalent oligosaccharides obtained through treatment with specific ferulic acid esterases, and a synthetic lignin-carbohydrate complex (LCC). Feruloyl substituents limited the hydrolysis of arabinoxylan and arabinan oligosaccharides but only if the feruloyl group was esterified to the terminal non-reducing arabinose. Somewhat surprisingly, the LCC-model compound, in which the arabinose residue is substituted with a bulky dilignol group, was degraded by the enzyme. This indicated that the enzyme is able to approach this linkage from the xylose side.
Luonteri
E
E
Biochemistry Department, Norwich Research Park, UK. elina.luonteri@vtt.fi
Kroon
P A
PA
Tenkanen
M
M
Teleman
A
A
Williamson
G
G
D001230:Aspergillus / Q000201:enzymology*; D002240:Carbohydrate Sequence; D002473:Cell Wall / Q000737:chemistry; D004187:Disaccharides / Q000302:isolation & purification / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000302:isolation & purification / Q000378:metabolism*; D010944:Plants / Q000737:chemistry; D014312:Trisaccharides / Q000302:isolation & purification / Q000378:metabolism