文章摘要
NMN转移酶和乙醇脱氢酶共固定化及其动力学特性
Co-immobilization conditions of NMN transferase and alcohol dehydrogenase and kinetics of co-immobilized double enzyme
投稿时间:2018-10-11  修订日期:2019-03-11
DOI:
中文关键词: 关键词:NADH  磁性纳米颗粒  NMN转移酶  乙醇脱氢酶  共固定化
英文关键词: Key words:NADH  magnetic nanoparticles  NMN transferase  alcohol dehydrogenase  co-immobilization
基金项目:
作者单位E-mail
余带兵 上海理工大学 医疗器械与食品学院 834426058@qq.com 
李红梅 上海理工大学 医疗器械与食品学院 sunnysand@126.com 
杨娟 上海理工大学 医疗器械与食品学院  
高露姣 东海水产研究所  
孙十凡 上海理工大学 医疗器械与食品学院  
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中文摘要:
      摘要:采用磁性纳米颗粒对NMN(烟酰胺单核苷酸)转移酶和乙醇脱氢酶进行共价共固定,用以生产NADH(烟酰胺腺嘌呤二核苷酸),并对共固定化条件、共固定化双酶酶学性质及其动力学进行了研究。实验结果显示双酶最佳共固定化反应条件为:NMN转移酶和乙醇脱氢酶添加量分别为6.5 U/0.5 mg和10.3 U/0.5 mg,体系pH控制在5.0~7.0条件下,25 ℃固定化2 h,NADH产率可达到87%,与游离酶73%的催化效率相比提高了14%。所得共固定化双酶在连续使用11次后,剩余酶活仍保留在61.1%左右,表明共固定化酶具有较好的操作稳定性。双酶动力方程推导与验证表明共固定化双酶反应体系符合米氏方程,其动力学反应速率取决于固定化乙醇脱氢酶的反应速率。
英文摘要:
      Abstract:NMN (nicotinamide mononucleotide) transferase and ethanol dehydrogenase were covalently immobilized with magnetic nanoparticles; to produce NADH (nicotinamide adenine dinucleotide). The conditions of co-immobilization, the properties and kinetics of co-immobilized enzyme were investigated. The optimized immobilization condition as follow : NMN transferase and alcohol dehydrogenase are 6.5 U/0.5 mg and 10.3 U/0.5 mg, respectively, and the system pH is controlled at 5.0-7.0 to immobilize the enymes for 2 h at 25℃, under which condition, NADH yield could reach 87%. After 11 reuses of the co-immobilized double enzyme, the residual enzyme activity still remains at about 61.1%, which showed a good operational stabilization. The deduction and validation of the kinetic equation of two enzymes showed that the reaction system of co-immobilized double enzymes accorded with Michaelis equation, and its kinetic reaction rate depended on the reaction rate of immobilized ethanol dehydrogenase.
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