Here,
lipase encapsulation is constructed by locking
enzyme molecules
in nanomolecular cages on the surface of SH-PEI@PVAC magnetic microspheres.
To improve the encapsulation efficiency in enzyme loading, the thiol
group is efficiently modified on the grafted polyethyleneimine (PEI)
using 3-mercaptopropionic acid. N2 adsorption–desorption
isotherms reveal the existence of mesoporous molecular cages on the
microsphere surface. The robust immobilizing strength of carriers
to lipase demonstrates the successful encapsulation of enzymes in
nanomolecular cages. The encapsulated lipase shows high enzyme loading
(52.9 mg/g) and high activity (51.4 U/mg). Different sizes of molecular
cages are established, and the cage size showed important effects
on lipase encapsulation. It shows that enzyme loading is low at a
small size of molecular cages, which is attributed to that the nanomolecular
cage is too small to house lipase. The investigation in lipase conformation
suggests that the encapsulated lipase retains its active conformation.
Compared with the adsorbed lipase, the encapsulated lipase shows higher
thermal stability (4.9 times) and higher resistance to denaturants
(5.0 times). Encouragingly, the encapsulated lipase shows high activity
and reusability in lipase-catalyzed synthesis of propyl laurate, suggesting
the potential application value of encapsulated lipase.
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