Analysis of the effect of metal ions on the ability of Xylanase to hydrolyze wheat bran by molecular dynamics simulations

Abstract

Introduction: Wheat bran is the main by-product of wheat processing, containing about 30% pentosan and 0.4%–0.7% ferulic acid. Wheat bran is the main raw material used to prepare feruloyl oligosaccharides by hydrolysis of Xylanase, we discovered that the ability of Xylanase to hydrolyze wheat bran could be affected in the presence of different metal ions.Methods: In the present study, we have probed the effects of different metal ions on the hydrolysis activity of Xylanase on wheat bran and tried to analyze the effect of Mn2+ and Xylanase by molecular dynamic (MD) simulation.Results: Our results suggested that Mn2+ had improved the Xylanase hydrolyzing wheat bran to obtain feruloyl oligosaccharides. Particularly when the concentration of Mn2+ reached 4 mmol/L, the optimal product has been obtained 2.8 times higher to compare with no addition. Through the MD simulation analysis, our results reveal that Mn2+ can induce structural change in the active site, which enlarges the substrate binding pocket. The simulation results also revealed that the addition of Mn2+ resulted in a low RMSD value compared with the absence of Mn2+ and helped stabilize the complex.Conclusion: Mn2+ could increase the enzymatic activity of Xylanase in the hydrolysis of feruloyl oligosaccharides in wheat bran. The finding could have significant implications for the preparation of feruloyl oligosaccharides from wheat bran.

Boosting sugarcane trash decomposition: synergistic action and proximity effect of xylanase and feruloyl esterase co-displayed on the cell surface of Pichia pastoris (Komagataella phaffi)

“…In previous studies, it has been reported that certain metal ions and organic reagents can enhance the activities of XYN 56,57 and FAE. 58 Therefore, in this study, we investigated the impact of additives on the activities of XYN and FAE on the P. pastoris cell surface.…”

“…The increase in XYN activity could be due to the structural change in the active site, resulting in the enlargement of substrate-binding pocket, induced by binding with the metal ion. 57 In contrast, the introduction of ethylenediaminetetraacetate (EDTA) had an adverse effect on XYN activity, resulting in a 35% reduction at the same 5 mM concentration. Additionally, the inclusion of 2-mercaptoethanol (2-ME) and dithiothreitol (DTT) showed a slight improvement in XYN activity, with increases of 12% and 16% at the 5 mM concentration, respectively (Table 3).…”

“…In previous studies, it has been reported that certain metal ions and organic reagents can enhance the activities of XYN 56,57 and Fig. 3 Temperature and pH stability of enzymes displayed on the cell surface of X-Pichia and F-Pichia.…”