Activation and stabilization of penicillin V acylase from streptomyces lavendulae in the presence of glycerol and glycols.
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.
Arroyo
M
M
Departamento de Bioquímica y Biología Molecular I, Facultad de Ciencias Biológicas, Universidad Complutense de Madrid, Spain.
Torres-Guzmán
R
R
de La Mata
I
I
Castillón
M P
MP
Acebal
C
C
D002384:Catalysis; D004789:Enzyme Activation; D004795:Enzyme Stability; D005990:Glycerol / Q000378:metabolism*; D006018:Glycols / Q000378:metabolism*; D010399:Penicillin Amidase / Q000378:metabolism*; D012997:Solvents; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature
D006018:Glycols; D012997:Solvents; D010399:Penicillin Amidase; D005990:Glycerol