Covalent Immobilization of Lipase on NH<sub>2</sub>-MIL-125(Ti) through Ugi Reaction for Biodiesel Production
In this study, heterogeneous biocatalysts were produced by successfully synthesizing the metal-organic framework (MOF) NH<sub>2</sub>-MIL-125(Ti) as a support, followed by the chemical stabilization of the lipase enzyme using the Ugi four-component reaction (Lipase-NH<sub>2</sub>-MIL-125), resulting in a stabilization efficiency of 87%. The amine group in MOF plays one of the reactants in the Ugi reaction, and a firm covalent bond is created between the enzyme and the support, which avoids enzyme leaching and leads to a stable biocatalyst. Enzyme efficiency, reusability, pH, and temperature stability of Lipase-NH<sub>2</sub>-MIL-125 have been investigated, and their high performance has been proven for the biocatalyst. The biodiesel production process using oleic acid has been utilized to evaluate the catalytic activity of the designed biocatalyst, and different parameters have been optimized. The results confirmed the good activity of Lipase-NH<sub>2</sub>-MIL-125 in biodiesel production, and even after 6 cycles, the activity slightly decreased, which confirmed the stability of the biocatalyst during the reaction.
Authors
- Valiollah Mirkhani (ORCID: https://orcid.org/0000-0001-7426-375X)
- Iraj Mohammadpoor‐Baltork (ORCID: https://orcid.org/0000-0001-7998-5401)
- Majid Moghadam (ORCID: https://orcid.org/0000-0001-8984-1225)
- Mehrnaz Bahadori
- Amir Landarani–Isfahani (ORCID: https://orcid.org/0000-0003-4252-4454)
- Shahram Tangestaninejad (ORCID: https://orcid.org/0000-0001-5263-9795)
- Ali Narimani
Institutions
- University of Isfahan (IR)
- Institute of Catalysis and Petrochemistry (RU)
Publication Details
- Journal
- ACS Applied Bio Materials
- Published
- 2025-05-27
- DOI
- https://doi.org/10.1021/acsabm.5c00321
- Citations
- 5
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 4.03