用于复杂生物聚合物水解的耐热植酸酶-木聚糖酶工程
Engineering of thermostable phytase-xylanase for hydrolysis of complex biopolymers.
作者信息
Patel Dharti K, Patel Kirankumar, Patel Darshan, Dave Gayatri
机构信息
PD Patel Institute of Applied Sciences, CHARUSAT, Changa, Anand, Gujarat 388421 India.
出版信息
3 Biotech. 2021 Aug;11(8):390. doi: 10.1007/s13205-021-02936-z. Epub 2021 Jul 29.
UNLABELLED
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 ( ) 108 °C, higher than the 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.
未标记
酶的工业加工需要更高的加热温度，这会影响酶的热稳定性并增加生产成本。在本研究中，木聚糖酶 - 植酸酶（XP）融合蛋白通过在具有冷休克启动子的单一载体中共表达产生，从而在最佳pH、温度下提高了活性以及蛋白质的热行为。通过差示扫描量热法（DSC）和热重分析（TGA）对木聚糖酶 - 植酸酶（XP）融合蛋白和植酸酶蛋白进行了表征。XP融合蛋白在高达124°C时热稳定，高于植酸酶，植酸酶在高达113.5°C时保持稳定。XP融合蛋白在其热转变中点（）108°C时表现出更高的稳定性，高于植酸酶的90°C。通过“融合蛋白”技术可以产生具有工业效率、环境友好、生产成本低且稳定性更高的蛋白质。
补充信息
在线版本包含可在10.1007/s13205-021-02936-z获取的补充材料。
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