Immobilization of the extracellular recombinant Lucky9 xylanase from Bacillus subtilis enhances activity at high temperature and pH

Sodium alginate beads were used as a carrier to immobilize a previously reported extracellular xylanase from Bacillus subtilis Lucky9 expressed in Escherichia coli. The optimal pH and the activity of the immobilized enzyme were increased at optimal temperature compared with the free enzyme. Our results suggest that the immobilized xylanase has potential applications in the biobleaching industry.
In the paper industry, chlorine is often used to treat the pulp for bleaching. After pulping, a large amount of xylan is present in the fiber. Xylanase can be used to degrade xylan in an eco‐friendly process called biobleaching, which can help minimize the usage of chlorine in the delignification process. However, a bottleneck in the adoption of biobleaching is the cost of xylanase and the requirement that xylanase be active and stable at extreme conditions. Here, we investigated whether using sodium alginate beads to immobilize an extracellular xylanase from Bacillus subtilis (Lucky9) can reduce the potential cost of enzyme usage. The optimal pH and the activity of the immobilized enzyme were increased at optimal temperature compared with the free enzyme. In addition, immobilized xylanase was shown to be more stable than free xylanase. The results of this study suggest that the immobilized xylanase has potential applications in the biobleaching industry.