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[目的]从1株生防细菌地衣芽孢杆菌SDYT-79中分离纯化出抑菌蛋白,并分析其理化性质。[方法]以地衣芽孢杆菌为材料,以不同硫酸铵饱和度确定最佳饱和度,然后通过Sephadex G-75凝胶层析柱分离出抗菌蛋白,经SDS-PAGE测定抗菌蛋白的分子质量,最后通过不同温度、酸碱度、保存时间、蛋白酶分析其稳定性。[结果]确定最佳饱和度为50%,经SephadexG-75层析柱洗脱出2个洗脱峰,峰Ⅰ具有抗菌活性,分子质量为107.931 KD。抗菌蛋白对温度、保存时间蛋白酶均不敏感,同时抗菌蛋白在中性和弱碱性条件下稳定性良好。[结论]抑菌蛋白具有较高的稳定性。
[Objective] The bacteriostatic protein was isolated and purified from an antimicrobial bacterium Bacillus licheniformis SDYT-79 and its physical and chemical properties were analyzed. [Method] With Bacillus licheniformis as material, the optimal saturation was determined by the saturation of different ammonium sulfate. The antimicrobial protein was separated by Sephadex G-75 gel column and the molecular mass of antimicrobial protein was determined by SDS-PAGE. Finally, Through the different temperature, pH, storage time, protease analysis of its stability. [Result] The optimal saturation was 50%. Two peaks were eluted by SephadexG-75 column. The peak I had antimicrobial activity and the molecular mass was 107.931 KD. Antibacterial proteins are insensitive to temperature and preservation time proteases, and antibacterial proteins have good stability under neutral and weak alkaline conditions. [Conclusion] The bacteriostatic protein has high stability.