Engineering of thermostable phytase-xylanase for hydrolysis of complex biopolymers.

Industrial processing of enzymes requires higher heating that affects the thermal stability of the enzyme and increases the production cost. In this study, xylanase-phytase (XP) fusion protein was generated via co-expression in a single vector with a cold-shock promoter, leading to improved activity at optimal pH, temperature and the thermal behaviour of the protein. Xylanase-phytase (XP) fusion and phytase proteins were characterized by differential scanning calorimetry (DSC) and thermogravimetric analysis (TGA). The XP fusion was thermally stable up to 124 °C, higher than phytase which was steady up to 113.5 °C. XP fusion exhibits higher stability at its thermal transition midpoint (T m) 108 °C, higher than the T m value of phytase which is 90 °C. Industrially efficient and environment-friendly proteins with low production cost and higher stability can be generated by 'fusion protein' technology. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13205-021-02936-z. © King Abdulaziz City for Science and Technology 2021.