Relative rates of hydrolysis by rat pancreatic lipase of esters of C2-C18 fatty acids with C1-C18 primary n-alcohols.
The rate at which rat pancreatic lipase (glycerol-ester hydrolase, EC 3.1.1.3) hydrolyzes the esters of primary n-alcohols containing from 1 to 18 carbon atoms with fatty acids containing from 2 to 18 carbon atoms was determined. The speed of hydrolysis was influenced, apparently independently, by both the acyl and the alkyl chains. With respect to the fatty acid moiety, the esters of dodecanoic acid were usually split at the most rapid rate. Esters of butyric acid were the next most susceptible. In the case of the alcohol moiety, esters of heptyl alcohol were hydrolyzed most rapidly. On the basis of the pattern of the relative rates of hydrolysis, it is proposed that the influence of the alcohol component is a result of its orienting the ester molecule at the oil/water interface. The fatty acid effect is attributed to enzyme-substrate specificity.
D000438:Alcohols; D000818:Animals; D002118:Calcium; D055598:Chemical Phenomena; D002621:Chemistry; D004952:Esters; D005227:Fatty Acids; D005230:Fatty Acids, Nonesterified; D005612:Freeze Drying; D007700:Kinetics; D008049:Lipase; D008956:Models, Chemical; D010189:Pancreatic Juice / Q000201:enzymology; D051381:Rats; D013499:Surface Properties
D000438:Alcohols; D004952:Esters; D005227:Fatty Acids; D005230:Fatty Acids, Nonesterified; D008049:Lipase; D002118:Calcium