Recent studies have confirmed that lipases become
activated through conformational rearrangements of
parts of the molecule which opens the active site upon
adsorption to an apolar interface [9e11]. Furthermore,
while the majority of proteins, as surface active
macromolecules, adsorb to interfaces by unfolding and
denaturation, lipases adsorb in a highly active state [12].
Adsorption studies of lipases have revealed that the
enzymes are also able to adsorb and to be activated at
a variety of hydrophobic and hydrophilic functionalized
liquid-crystalline solid surfaces (SAMs) [13].