Synthesis and Characterization of Porous Polymer as a Support Matrix for Lipase Immobilization

Authors

  • Erwanto Erwanto Universitas Bojonegoro, Indonesia http://orcid.org/0000-0002-1043-6049
  • Arya Ananda Saputra Department of Chemistry, Faculty of Science and Technology, Universitas Bojonegoro, Jl. Lettu Suyitno No.02 Kalirejo, Bojonegoro, Indonesia , Indonesia
  • Muhammad Rakha Abimanyu Department of Chemistry, Faculty of Science and Technology, Universitas Bojonegoro, Jl. Lettu Suyitno No.02 Kalirejo, Bojonegoro, Indonesia, Indonesia

DOI:

https://doi.org/10.33394/hjkk.v13i4.16864

Keywords:

Lipase, immobilization, porous polymer, porogen, glycidyl methacrylate.

Abstract

Immobilization of lipase on solid supports has become a promising approach to improve enzyme stability, activity, and reusability in various industrial processes. This study focuses on the development of a porous polymer, poly(glycidyl methacrylate-co-trimethylolpropane trimethacrylate) [Poly(GM-co-TT)], as a functional support for covalent lipase immobilization. The experimental procedure included three main stages. First, Poly(GM-co-TT) was synthesized via free radical polymerization using a ternary porogenic solvent system consisting of 1,4-butanediol, 1-propanol, and water in a 4:7:1 (v/v) ratio to obtain a porous structure. Second, lipase was immobilized covalently through the reaction between epoxy groups of the polymer and amino groups of the enzyme, using a 0.2 M KCl–NaOH buffer (pH 11) at a final enzyme concentration of 10 mg/mL, incubated at room temperature for 120 minutes. Third, characterization was performed using FTIR spectroscopy and scanning electron microscopy (SEM) to verify successful immobilization. FTIR analysis revealed the presence of ester (C=O), ether (C–O–C), and epoxide (C–O) groups in the polymer. Post-immobilization spectra showed reduced epoxy band intensity (~910 and 840 cm⁻¹) and the appearance of amide bands (~1640–1660 cm⁻¹), indicating covalent bonding between polymer and enzyme. SEM images confirmed a porous, globular, interconnected morphology with well-distributed pores, ideal for enzyme anchoring. The open and rough surface increases surface area, enhancing immobilization efficiency. The novelty of this study lies in employing Poly(GM-co-TT) as a porous polymer that preserves epoxy functionality while effectively supporting covalent lipase immobilization.

References

Amalia, S., Angga, S. C., Iftitah, E. D., Septiana, D., Anggraeny, B. O. D., Warsito, Hasanah, A. N., & Sabarudin, A. (2021). Immobilization of trypsin onto porous methacrylate-based monolith for flow-through protein digestion and its potential application to chiral separation using liquid chromatography. Heliyon, 7(8), e07707. https://doi.org/10.1016/j.heliyon.2021.e07707

Giraldo, L., Gómez-Granados, F., & Moreno-Piraján, J. C. (2023). Biodiesel Production Using Palm Oil with a MOF-Lipase B Biocatalyst from Candida Antarctica: A Kinetic and Thermodynamic Study. International Journal of Molecular Sciences, 24(13). https://doi.org/10.3390/ijms241310741

Hasanah, A. N., Maelaningsih, F. S., Apriliandi, F., & Sabarudin, A. (2020). Synthesis and Characterisation of a Monolithic Imprinted Column Using a Methacrylic Acid Monomer with Porogen Propanol for Atenolol Analysis. Journal of Analytical Methods in Chemistry, 2020, 1–15. https://doi.org/10.1155/2020/3027618

Lyu, X., Gonzalez, R., Horton, A., & Li, T. (2021). Immobilization of Enzymes by Polymeric Materials. Catalysts, 11(1211), 1–15. https://doi.org/https:// doi.org/10.3390/catal11101211

Maghraby, Y. R., El-shabasy, R. M., Ibrahim, A. H., & Azzazy, H. M. E. (2023). Enzyme Immobilization Technologies and Industrial Applications. ACS Omega, 8, 5184–5196. https://doi.org/10.1021/acsomega.2c07560

Mandari, V., & Kumar, S. (2022). Biodiesel Production Using Homogeneous , Heterogeneous , and Enzyme Catalysts via Transesterification and Esterification Reactions : a Critical Review. BioEnergy Research, 935–961. https://doi.org/10.1007/s12155-021-10333-w

Miletic, N., Rohandi, R., Vukovic, Z., & Nastasovic, A. (2009). Surface modification of macroporous poly ( glycidyl methacrylate- co -ethylene glycol dimethacrylate ) resins for improved Candida antarctica lipase B immobilization. Reactive & Functional Polymers, 69(2009), 68–75. https://doi.org/10.1016/j.reactfunctpolym.2008.11.001

Sabarudin, A., Shu, S., Yamamoto, K., & Umemura, T. (2021). Preparation of metal-immobilized methacrylate-based monolithic columns for flow-through cross-coupling reactions. Molecules, 26(23), 1–14. https://doi.org/10.3390/molecules26237346

Sarmah, N., Revathi, D., Rani, Y. . ., Sridhar, S., Mehtab, V., & Sumana, C. (2017). Recent Advances on Sources and Industrial Applications of Lipases. Biotechnology Progress, 34(5–18), 1–67. https://doi.org/10.1002/btpr.2581

Septiana, D., Angga, S. C., Amalia, S., Iftitah, E. D., & Sabarudin, A. (2018). Modification of monolithic stationary phase using human serum albumin as chiral separation. AIP Conference Proceedings, 2021(2018). https://doi.org/10.1063/1.5062754

Xie, W., & Huang, M. (2020). Fabrication of immobilized Candida rugosa lipase on magnetic Fe3O4-poly(glycidyl methacrylate-co-methacrylic acid) composite as an efficient and recyclable biocatalyst for enzymatic production of biodiesel. Renewable Energy, 158, 474–486. https://doi.org/10.1016/j.renene.2020.05.172

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Published

2025-08-31

How to Cite

Erwanto, E., Saputra, A. A., & Abimanyu, M. R. (2025). Synthesis and Characterization of Porous Polymer as a Support Matrix for Lipase Immobilization. Hydrogen: Jurnal Kependidikan Kimia, 13(4), 743–751. https://doi.org/10.33394/hjkk.v13i4.16864

Issue

Vol. 13 No. 4 (2025): August 2025

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