Studies on the degradation pattern of wheat malt endo-1,4-β-xylanase on wheat-derived arabinoxylans.

Abstract

Wheat malt endo-1,4-β-xylanase is a key enzyme for arabinoxylan degradation, but its wheat-derived arabinoxylan degradation pattern is unclear. Water-extractable arabinoxylan (WEAX) of 300-750 kDa and 30-100 kDa were the two components with the highest degradation efficiency of wheat malt endo-1,4-β-xylanase, followed by > 1000 kDa WEAX, but 100-300 kDa WEAX showed the lowest degradation efficiency. The main enzymatic products were the 5-30 kDa WEAX, which accounted for 57.57%, 68.15%, and 52.28% of WAXH, WAXM, and WAXL products, respectively. The enzymatic efficiency of wheat malt endo-1,4-β-xylanase was relatively high, and the continuity of enzymatic efficiency was good, especially since the enzymatic reaction was the most intense in 1-3 h. WEAX of > 300 kDa was highly significant and positively correlated with viscosity. In comparison, WEAX of < 30 kDa was highly significant and negatively correlated with viscosity. As the enzymatic degradation proceeded, there were fewer and fewer macromolecular components but more and more small molecule components, and the system viscosity became smaller and smaller. In this study, it was found that wheat malt endo-1,4-β-xylanase degraded preferentially 300-750 kDa and 30-100 kDa WEAX, not in the order of substrate size in a sequential enzymatic degradation. Wheat malt endo-1,4-β-xylanase was most efficient within 3 h, primarily generating < 30 kDa WEAX ultimately. The main products were highly significantly negatively correlated with the system viscosity, so that the system viscosity gradually decreased as the enzymatic hydrolysis proceeded. © 2024 Society of Chemical Industry.