Enzyme immobilization beyond the Biocatalysis Department at Institute of Catalysis and Petroleum Chemistry (ICP-CSIC): Advances in design and synthesis of support materials
Year: 2026
Type: article
Abstract: Enzyme immobilization as a subject of study was established by Professor Antonio Ballesteros at the newly established Institute of Catalysis and Petroleum Chemistry, ICP, upon his return from his stay in the United States in the late 1970s. In the early stages, agarose was used as a support material, which gave rise to a line of research within the Institute’s Biocatalysis Department. The variety of materials as supports for enzymes described along the last decades ranges from inorganic materials like silica or alumina), various biological materials (chitosan, vegetable fibers) to a wide variety of synthetic polymers. The expertise in the design, synthesis and characterization of materials offered by ICP members beyond this Department was seen as an extraordinary opportunity for synergy in this field. Thus, new materials were searched, designed, developed, and used as matrices over time, expanding the range of biocatalysts with different properties and potential uses. This work provides a modest overview of how tailor-made designed materials can provide new insights and enable different strategies for enzyme immobilization to obtain biocatalysts with improved properties. From the basis of commercial ones like agarose for covalent attachment, or amorphous silica for noncovalent binding, tailor-made materials have been designed and synthetized. Particularly ordered mesoporous materials (OMM) for noncovalent immobilization or metal organic frameworks (MOFs) for “in situ” (or one-pot) immobilization. With this two families of materials joint advantages of covalent and non-covalent strategies of enzyme immobilization can be achieved. This is high enzyme loading where leaching is prevented, activity can be preserved and stability can be improved.
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
OpenAlex ID: W7165764103