Arroyo M, Torres-Guzmán R, de La Mata I, Castillón M P, Acebal C
Departamento de Bioquímica y Biología Molecular I, Facultad de Ciencias Biológicas, Universidad Complutense de Madrid, Spain.
Biotechnol Prog. 2000 May-Jun;16(3):368-71. doi: 10.1021/bp000023h.
Penicillin V acylase (EC 3.5.1.11) from Streptomyces lavendulae showed both enhanced activity and stability in mixed water/glycerol and water/glycols solvents. The catalytic activity was increased up to a critical concentration of these cosolvents, but further addition of the latter led to a gradual protein deactivation. The highest stabilizing effect was achieved in the presence of glycerol. Thermal stability was increased proportionally to the concentration of glycerol and glycols in the reaction mixture only if the amount added is below the threshold concentration. Reaction conditions that allow simultaneously enhanced activity and stability in the hydrolysis of penicillin V catalyzed by penicillin V acylase from S. lavendulae could be established.
来自薰衣草链霉菌的青霉素V酰基转移酶（EC 3.5.1.11）在水/甘油和水/二醇混合溶剂中表现出增强的活性和稳定性。催化活性在这些助溶剂的临界浓度之前会增加，但进一步添加助溶剂会导致蛋白质逐渐失活。在甘油存在下可实现最高的稳定效果。仅当添加量低于阈值浓度时，热稳定性才与反应混合物中甘油和二醇的浓度成比例增加。可以建立使来自薰衣草链霉菌的青霉素V酰基转移酶催化青霉素V水解时同时增强活性和稳定性的反应条件。
