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.

酶的工业加工需要较高的加热，这会影响酶的热稳定性并增加生产成本。在这项研究中，木聚糖酶-植酸酶 (XP) 融合蛋白是通过在单个载体中与冷休克启动子共表达产生的，从而提高了蛋白质在最佳 pH 值、温度和热行为下的活性。木聚糖酶-植酸酶 (XP) 融合蛋白和植酸酶蛋白通过差示扫描量热法 (DSC) 和热重分析 (TGA) 进行表征。XP 融合在高达 124 °C 时是热稳定的，高于在高达 113.5 °C 时稳定的植酸酶。XP fusion 在其热转变中点 ( T _m ) 108 °C 处表现出更高的稳定性，高于T _m植酸酶值为 90 °C。“融合蛋白”技术可以生产出工业高效、环境友好、生产成本低、稳定性高的蛋白质。