Lipoprotein Lipase an overview

sn
-1, sn-2 and sn-3.
The action of LPL involves two distinct steps. First,
the enzyme adsorbs at the lipid–water interface;
then, in the second step, the enzyme seeks out a
single substrate molecule at the interface, aligns at
the active site and hydrolyses it:
Lipolysis in milk leads to the preferential release of
short- and medium-chain fatty acids. Triglycerides
probably orient at the lipid–water interface,
thereby positioning short chain fatty acids for
hydrolysis. LPL also catalyses the formation of ester
bonds. Therefore, it is transacylase. In the formation
of ester bonds, fatty acids are substrates for LPL and
are incorporated into di- and triglycerides.
The binding of LPL to the milk fat globules as
substrate is pH-dependent, occurring optimally at
∼pH 8. LPL also binds to a variety of lipid structures
such as liposomes and lipoproteins. Binding is rapid
and reversible and is mediated by a lipid-binding
site, resulting in stabilization of the enzyme.
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