Importance of enzyme and solvent physical properties for the biocompatibility relationship of alpha-amino acid ester hydrolase.
The enzyme alpha-amino acid ester hydrolase was used with a variety of organic solvents to further explore the relationships between biocompatibility and solvent physical properties. Biocompatibility was shown to be system-specific; that is, the infection point of the characteristic log P trend (approximately 1.5) was specific to the enzyme employed, while the biocompatibility of solvents that were exceptions to the trend was dependent on the extent of agitation. In addition, phase toxic solvents all possessed a high interfacial tension with water. Finally, while the source of the enzyme may be significant, the extent of purification does not appear to be a factor in biocompatibility.
MacNaughtan
M D
MD
Department of Chemical Engineering, Queen's University, Kingston, Canada.
Daugulis
A J
AJ
D001711:Biotransformation / Q000187:drug effects; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002384:Catalysis; D002506:Cephalexin / Q000493:pharmacokinetics*; D005069:Evaluation Studies as Topic; D006868:Hydrolysis; D011489:Protein Denaturation; D012997:Solvents / Q000494:pharmacology
D012997:Solvents; D002265:Carboxylic Ester Hydrolases; C058058:alpha-amino acid esterase; D002506:Cephalexin