Preparation of Proline-Modified UIO−66 Nanomaterials and Investigation of Their Potential in Lipase Immobilization

Dong, Xiaoxiao; Zhang, Chengnan; Patil, Prasanna J.; Li, Weiwei; Li, Xiuting

doi:10.3390/catal14030180

Cited by 1 publication

(1 citation statement)

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“…While it is expected that the surface area and porosity decrease after immobilization, the slight increase in pore diameter suggests that the immobilization may have resulted in an expansion of the pore size of the mesoporous structures, which may have been beneficial to mass transport in the hydrolysis process or could be associated with micropore obstruction or clogging by the enzyme. Similar observation with increased pore size after enzyme immobilization has been reported. − …”

Section: Resultssupporting

confidence: 88%

Alloyed Trimetallic Nanocomposite as an Efficient and Recyclable Solid Matrix for Ideonella sakaiensis Lipase Immobilization

Addai,

Wu,

Lin

et al. 2024

Langmuir

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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.

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Section: Resultssupporting

confidence: 88%