Enzyme-catalyzed processes in organic solvents.
Three different lipases (porcine pancreatic, yeast, and mold) can vigorously act as catalysts in a number of nearly anhydrous organic solvents. Various transesterification reactions catalyzed by porcine pancreatic lipase in hexane obey Michaelis-Menten kinetics. The dependence of the catalytic activity of the enzyme in organic media on the pH of the aqueous solution from which it was recovered is bell-shaped, with the maximum coinciding with the pH optimum of the enzymatic activity in water. The catalytic power exhibited by the lipases in organic solvents is comparable to that displayed in water. In addition to transesterification, lipases can catalyze several other processes in organic media including esterification, aminolysis, acyl exchange, thiotransesterification, and oximolysis; some of these reactions proceed to an appreciable extent only in nonaqueous solvents.
D000438:Alcohols / Q000378:metabolism; D000818:Animals; D002175:Candida / Q000201:enzymology; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D009089:Mucor / Q000201:enzymology; D010179:Pancreas / Q000201:enzymology; D012997:Solvents; D013329:Structure-Activity Relationship; D013552:Swine; D014280:Triglycerides / Q000378:metabolism; D014867:Water
D000438:Alcohols; D012997:Solvents; D014280:Triglycerides; D014867:Water; D008049:Lipase