Maleic anhydride-modified xylanase and its application to the clarification of fruits juices.

At presently, the catalytic activity of xylanase is sub-optimal, and the required reaction conditions are harsh. To improve its catalytic activity and stability, xylanase (XY) was chemically modified with maleic anhydride (MA). The enzymatic properties of this maleic anhydride-modified xylanase (MA-XY) were then evaluated and analyzed spectroscopically. The results showed that the thermal stability, use of organic solvents, storage stability and the pH range of 3.0 to 9.0 for MA-XY were better than that for XY alone. The kinetic parameters of the enzyme (K values) decreased from 40.63 to 30.23 mg/mL. Spectroscopic analysis showed that XY had been modified by the acylation reaction to become a tertiary structure. An assay based on clarifying fruit juices showed that the clarification capacity and reducing sugar content using MA-XY increased compared with those using XY. Overall, this study provides a theoretical basis for improving the application of XY in the food industry.