摘要
用初速度法测定了青霉素酰化酶基因工程菌 E.coli A_(56)(pPA22)游离细胞和固定化细胞水解青霉素 G 的动力学常数,并进行了动力学模型的检验。该菌体酶活高,米氏常数小,固定化后米氏常数和苯乙酸抑制常数增大,底物抑制常数和6-APA 抑制常数没有变化。通过青霉素 G 裂解过程的考察,验证了青霉裂解动力学模型的适用性及动力学常数测定的可靠性。
By means of initial rate measurement,the determination of kinetic parameters and discrimination of the model were performed for the hydrolysis of penicillin G by free and immobilized recombinant E.coil A_(56)(pPA22)cells that produce penicillin acylase.The activity of E·coli A_(56)(pPA22)cells was higher and the Michaelis constant was smaller.When the ceils were immobilized,the Michaelis constant and the inhibition constant for PAA were increased,but the inhibition constants for substrate and 6-APA had no changes.By investigation on the process of penicillin hydrolysis,the adaptability of kinetic model and the reliability of kinetic parameters have been confirmed.
出处
《化学反应工程与工艺》
CAS
CSCD
北大核心
1991年第3期224-229,共6页
Chemical Reaction Engineering and Technology
基金
中国科学院基金
关键词
青霉素G
水解
动力学
Penicillin G
Hydrolysis
Kinetics
