Improvement the thermostability and specific activity of acidic xylanase PjxA from Penicillium janthinellum via rigid flexible sites.

Abstract excerpt

Acidic xylanase PjxA from Penicillium janthinellum MA21601, with good eosinophilic and enzymatic activity, is an excellent candidate for xylan degradation to achieve effective utilization of biomass materials. However, the low thermal stability of PjxA has become a major bottleneck in its application. In this study, the flexible sites of PjxA were identified and rigidified through computational simulations of...

Topics

• Penicillium
• Enzyme Stability
• Endo-1,4-beta Xylanases
• Temperature
• Catalytic Domain
• Models, Molecular
• Kinetics
• Mutation