Enological pectinase immobilized on polymer microparticles as efficient biocatalysts for wine clarification

• Author(s): Denchev, Z. ; Oliveira, Sandra Cristina Gomes ; Araújo, Samuel ; Dencheva, Nadya Vasileva
• Date: 2024
• Persistent ID: https://hdl.handle.net/1822/94204
• Origin: RepositóriUM - Universidade do Minho
• Document Type: Other
• Language: English
• Contributor(s): Universidade do Minho

Description

One of the key areas of polymer biotechnology is the use of high molecular weight compounds as supports for enzymes, enhancing their utility in industrial applications. Free pectinase is commonly employed as a biocatalyst in wine clarification; however, its removal, recovery, and reuse are not feasible. To address these limitations, this study focuses on the immobilization of a commercial pectinolytic preparation (Pec) onto highly porous polymer microparticles (MP). Seven microparticulate polyamide (PA) supports, namely PA4, PA6, PA12 (with and without magnetic properties), and the copolymeric PA6-12 MP, were synthesized via activated anionic polymerization of various lactams. Pectinase was non-covalently immobilized on these supports through adsorption, forming Pec@PA conjugates. Comparative activity and kinetic studies revealed that the Pec@PA12 conjugate exhibited more than twice the catalytic efficiency of the free enzyme, followed by Pec@PA6-Fe and Pec@PA4-Fe. All Pec@PA complexes were tested in the clarification of industrial rosé must, demonstrating faster performance compared to the free enzyme. Some immobilized biocatalysts supported up to five consecutive reuse cycles, maintaining up to 60% of their initial activity and achieving complete clarification within 3–36 hours. These findings highlight the potential for industrial application of non-covalently immobilized pectinase on various polyamide microparticles, with possibilities for customization of the conjugates' properties.