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Inhibition of staphylococcus aureus lipase activity by alcohol
Author(s) -
Mates A.
Publication year - 1973
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532710
Subject(s) - alcohol , chemistry , lipase , substrate (aquarium) , hydrolysis , enzyme , triacylglycerol lipase , inhibitory postsynaptic potential , staphylococcus aureus , adsorption , organic chemistry , biochemistry , bacteria , biology , ecology , genetics , neuroscience
A series of saturated n ‐primary alcohols has been examined for its inhibitory effect on staphylococcal lipase. The efficiency of the inhibition of hydrolysis of the triglycerides increased with the chain length of the alcohol and reached a maximum of seven carbon atoms. Further increases in the chain length caused a decrease in the inhibitory ability of the alochol. However the efficiency of the inhibitory effect on Tween 80 hydrolysis increased with the chain length up to 12 carbon atoms. The degree of inhibition caused with the removal of the hydroxyl group away from the end of the chain. The similar keto compounds were more effective than were the alochol compounds. The effect of the alcohols on the enzyme activity could be overcome by addition of more substrate. Evidence is presented that shows that the inhibiting activity of the alcohol is due to its adsorption onto the substrate, thus blocking the enzyme from the substrate.