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Updated: Oct 22, 2025
High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
Published on: September 20, 2016
Engineering of thermostable phytase-xylanase for hydrolysis of complex biopolymers
Dharti K Patel1, Kirankumar Patel1, Darshan Patel1
1PD Patel Institute of Applied Sciences, CHARUSAT, Changa, Anand, Gujarat 388421 India.
Abstract:
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.
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