| Title : Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger - Ralet_1994_Carbohydr.Res_263_257 |
| Author(s) : Ralet MC , Faulds CB , Williamson G , Thibault JF |
| Ref : Carbohydr Res , 263 :257 , 1994 |
| Abstract : The activity of two forms of ferulic acid esterase (FAE) from Aspergillus 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 specificities for the various feruloylated substrates and were more active on certain substrates of cell-wall origin than on methyl ferulate. Both enzymes preferred the arabinose residue to which ferulic acid is attached in the furanose form. FAE-I had no clear preference for the type of linkage 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 Ara f ring while no catalysis was observed when ferulic acid was attached to O-2. Both enzymes showed maximum activity on feruloylated trisaccharides. An increase in the length of the oligosaccharide chain did not preclude catalysis, but feruloylated oligosaccharides of a dp > 3 were hydrolysed at a reduced rate. Our results support the hypothesis that different kinds of ferulic acid esterases exist with different specificities for the oligosaccharide chain of the feruloylated substrates. |
| ESTHER : Ralet_1994_Carbohydr.Res_263_257 |
| PubMedSearch : Ralet_1994_Carbohydr.Res_263_257 |
| PubMedID: 7805053 |
| Gene_locus related to this paper: aspng-faeb , aspni-FAEA |
| Gene_locus related to this paper: aspng-faeb , aspni-FAEA |
Ralet MC, Faulds CB, Williamson G, Thibault JF (1994)
Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger
Carbohydr Res
263 :257
Ralet MC, Faulds CB, Williamson G, Thibault JF (1994)
Carbohydr Res
263 :257