Enzyme action in polymer and salt solutions. I. Stability of penicillin acylase in poly(ethylene glycol) and potassium phosphate solutions in relation to water activity.
The stability of penicillin acylase (penicillin aminohydrolase, EC 3.5.1.11) was studied in poly(ethylene glycol) and potassium phosphate solutions. Enzyme stability measured as the half-life of the enzymatic activity and the transition temperature determined by differential scanning calorimetry, correlated well. The enzyme stability could not be related to the water activity as a measure of solute-solvent interaction. It seems to be related more to the concentration of the solutes and much less to the molecular weight of poly(ethylene glycol). The stabilizing effect of poly(ethylene glycol) is also discussed in terms of poly(ethylene glycol)-protein interactions.
D000581:Amidohydrolases / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D004355:Drug Stability; D006207:Half-Life; D010399:Penicillin Amidase / Q000378:metabolism*; D010710:Phosphates; D011092:Polyethylene Glycols; D011188:Potassium; D017680:Potassium Compounds; D012996:Solutions; D012997:Solvents; D013816:Thermodynamics; D014867:Water
D010710:Phosphates; D017680:Potassium Compounds; D012996:Solutions; D012997:Solvents; D014867:Water; D011092:Polyethylene Glycols; C013216:potassium phosphate; D000581:Amidohydrolases; D010399:Penicillin Amidase; D011188:Potassium