【摘要】 本文对谷氨酸生产茵AS₁.299谷氨酸脱氢酶的专一性辅酶、热稳定性、动力学参数和发酵过程中的活力变化进行的研究表明,该酶以辅酶Ⅱ为其专一性辅酶;于50℃保温10分钟保留活力约为18％,而在60℃保温同样时间几乎完全失活;对L-谷氨酸和辅酶Ⅱ的动力学参数分别为55.6和0.139毫克分子;在发酵过程中,前期酶活力逐渐上升,在24小时左右酶活力最高,其后酶活力逐渐下降。更多还原

【Abstract】 In this paper, specifie coenzyme, thermolability, kinetic parameters, and activity change during fermentation for glutamate dehydrogenase in glutamate-produced bacteria AS1. 299 was studied.It was shown that CoⅡ other than CoⅠ was the specific coenzyme of the glutamate dehydrogenase. The enzyme is thermolabile. The enzymatic activity remains to be 18% after incubation at 50℃ for 10 min, and the activity is completely lost after incubation at 60℃ for 10 min. The kinetic parameters for L-glutamate and CoⅡ of the enzyme are 55.6 and 0.139 mM respectively. During initial fermentation the enzymatic activity raises gradually, it reaches the maximum in about 24 hours and then decreases.更多还原