In
this work, a trimetallic (Ni/Co/Zn) organic framework (tMOF),
synthesized by a solvothermal method, was calcinated at 400 and 600
°C and the final products were used as a support for lipase immobilization.
The material annealed at 400 °C (Ni-Co-Zn@400) had an improved
surface area (66.01 m2/g) and pore volume (0.194 cm3/g), which showed the highest enzyme loading capacity (301
mg/g) with a specific activity of 0.196 U/mg, and could protect the
enzyme against thermal denaturation at 65 °C. The optimal pH
and temperature for the lipase were 8.0 and 45 °C but could tolerate
pH levels 7.0–8.0 and temperatures 40–60 °C. Moreover,
the immobilized enzyme (Ni-Co-Zn@Lipase, Ni-Co-Zn@400@Lipase, or Ni-Co-Zn@600@Lipase)
could be recovered and reused for over seven cycles maintaining 80,
90, and 11% of its original activity and maintained a residual activity
>90% after 40 storage days. The remarkable thermostability and
storage
stability of the immobilized lipase suggest that the rigid structure
of the support acted as a protective shield against denaturation,
while the improved pH tolerance toward the alkaline range indicates
a shift in the ionization state attributed to unequal partitioning
of hydroxyl and hydrogen ions within the microenvironment of the active
site, suggesting that acidic residues may have been involved in forming
an enzyme–support bond. The high enzyme loading capacity, specific
activity, encouraging stability, and high recoverability of the tMOF@Lipase
indicate that a multimetallic MOF could be a better platform for efficient
enzyme immobilization.