Mc. Ralet et al., DEGRADATION OF FERULOYLATED OLIGOSACCHARIDES FROM SUGAR-BEET PULP ANDWHEAT BRAN BY FERULIC ACID ESTERASES FROM ASPERGILLUS-NIGER, Carbohydrate research, 263(2), 1994, pp. 257-269
The activity of two forms of ferulic acid esterase (FAE) from Aspergil
lus niger on a synthetic feruloylated substrate (methyl ferulate) and
on 11 different feruloylated oligosaccharides from sugar-beet pulp and
wheat bran was determined. The enzymes exhibited different specificit
ies for the various feruloylated substrates and were more active on ce
rtain substrates of cell-wall origin than on methyl ferulate. Both enz
ymes preferred the arabinose residue to which ferulic acid is attached
in the furanose form. FAE-I had no clear preference for the type of l
inkage involved between the ferulic acid units and the oligosaccharide
chain. In contrast, FAE-III had a clear requirement for ferulic acid
to be attached to O-5 of the Araf ring while no catalysis was observed
when ferulic acid was attached to O-2. Both enzymes showed maximum ac
tivity on feruloylated trisaccharides. An increase in the length of th
e oligosaccharide chain did not preclude catalysis, but feruloylated o
ligosaccharides of a dp > 3 were hydrolysed at a reduced rate. Our res
ults support the hypothesis that different kinds of ferulic acid ester
ases exist with different specificities for the oligosaccharide chain
of the feruloylated substrates.