Synergy between enzymes involved in the degradation of insoluble wheat flour arabinoxylan

Abstract

Two microbial endo-β-1,4-xylanases (EXs, EC 3.2.1.8) belonging to glycanase families 10 and 11 were examined for their ability to release ferulic acid (FA) from water-unextractable arabinoxylan (WU-AX) in the presence of a feruloyl esterase (FoFAE-II) from Fusarium oxysporum. WU-AX was incubated with different levels of a Thermoascus aurantiacus family 10 (XYLI) and a Sporotrichum thermophile family 11 (XYLA) endoxylanases. At 10 g/l arabinoxylan, enzyme concentrations ( K E values) needed to obtain half-maximal hydrolysis rates for FA release were 0.18 and 0.44 nM for the xylanases from T. aurantiacus and S. thermophile, respectively. Determination of V max/ K E revealed that the family 10 enzyme performed 4.3 times more efficiently than the family 11 enzyme in liberation of FA when a feruloyl esterase is present. Molecular weights of the products formed were assessed and separation of feruloyl-oligosaccharides was achieved by anion-exchange and size-exclusion chromatography (SEC). The results showed that the degradation of the xylan backbone was influenced strongest by the action of xylanases while the presence of the esterase mainly resulted in the release of ferulic acid from the produced short chain feruloylated xylo-oligosaccharides by the action of xylanases.