Document Detail

Relative rates of hydrolysis by rat pancreatic lipase of esters of C2-C18 fatty acids with C1-C18 primary n-alcohols.
MedLine Citation:
PMID:  5802639     Owner:  NLM     Status:  MEDLINE    
The rate at which rat pancreatic lipase (glycerol-ester hydrolase, EC 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.
F H Mattson; R A Volpenhein
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of lipid research     Volume:  10     ISSN:  0022-2275     ISO Abbreviation:  J. Lipid Res.     Publication Date:  1969 May 
Date Detail:
Created Date:  1969-09-30     Completed Date:  1969-09-30     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0376606     Medline TA:  J Lipid Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  271-6     Citation Subset:  IM    
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MeSH Terms
Chemical Phenomena
Fatty Acids*
Fatty Acids, Nonesterified
Freeze Drying
Models, Chemical
Pancreatic Juice / enzymology
Surface Properties
Reg. No./Substance:
0/Alcohols; 0/Esters; 0/Fatty Acids; 0/Fatty Acids, Nonesterified; 7440-70-2/Calcium; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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