Effect of an endo-1,4-β-xylanase from wheat malt on water-unextractable arabinoxylan derived from wheat

Non-starch polysaccharides in wheat are dominated by arabinoxylan (AX). Endo-1,4-β-xylanase (EC 3.2.1.8) is the most important enzyme for degrading AX. This paper investigated the ability of endo-1,4-β-xylanase extracted from wheat malt to degrade non-water-extractable wheat-derived arabinoxylan (WUAX).

The enzyme was observed to break down wheat-derived WUAX effectively, substantially increasing the concentration of water-extractable arabinoxylan (WEAX) in the system for up to 6 h. A considerable quantity of arabinose xylooligosaccharide (AXOS) was also produced, suggesting that the enzyme could produce oligosaccharides too. The molecular weight of the product WEAX was between 23 and 27 kDa and the content of oligosaccharides changed with degradation time. This suggests that endo-1,4-β-xylanase can not only degrade WUAX into WEAX and xylooligosaccharides but can also degrade the xylooligosaccharides with larger molecular weights into xylobiose and xylotriose. The viscosity of the degradation product increased significantly in the first 2 h, then decreased with longer degradation times. The concentration of WEAX in the reaction system increased throughout the reaction but at gradually lower rates, indicating that the endo-1,4-β-xylanase degraded WEAX better than it degraded WUAX. Rheological tests showed that solutions prepared from the WEAX that was produced had properties of a pseudoplastic fluid.

The results showed that the wheat malt endo-1,4-β-xylanase, which we had previously tested on WEAX, was also effective in degrading wheat-derived WUAX. This study can therefore provide a theoretical basis for the subsequent role of the enzyme in other sources of xylan, and provide guidance for the quality control of beer in the brewing process. © 2021 Society of Chemical Industry.