A caveat for the use of log P values for the assessment of the biocompatibility of organic solvents

• Published in: Biotechnology letters Vol. 24; no. 11; pp. 857 - 860
• Main Authors: POGOREVC, Mateia, STECHER, Hartmut, FABER, Kurt
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01.06.2002; Springer Nature B.V
• Subjects: Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Organic solvents; Solvents; Pseudomonadales; Mandelate racemase; Deactivation; Yeast; Enzyme; Triacylglycerol lipase; Esterases; Lyases; Partition coefficient; Pseudomonas; Carboxylic ester hydrolases; Fungi; Organic solvent; Isomerases; Enzymatic activity; Biotransformation; Bacteria; Hydrolases; Pseudomonadaceae; Biocompatibility; Fungi Imperfecti; Candida rugosa; Thallophyta
• ISSN: 0141-5492; 1573-6776
• DOI: 10.1023/A:1015598523282

The degree of enzyme deactivation for lipases from Candida rugosa and Pseudomonas sp., hydroxynitrile lyase and mandelate racemase upon exposure to organic solvents can be correlated to their respective partition coefficients (log P values). However, three unexpected results were obtained: (1) the deactivation exerted by protic solvents, e.g., methanol, is severely underestimated; (2) little deactivation by an organic solvent cannot neccessarily be correlated to catalytic activity in this medium, and (3) in contrast to other enzymes, hydroxynitrile lyase is exceptionally stable towards deactivation by DMF.[PUBLICATION ABSTRACT]