- Article
Efficient Immobilization of Lipase in Porous Polymer for Catalysis and Optimization of Esterification by Response Surface Methodology
- Eliézer Luz do Espírito Santo,
- Sabryna Couto Araujo and
- Julieta Rangel de Oliveira
- + 5 authors
Flavor esters are valuable compounds widely used in the food, beverage, and cosmetics industries for their aroma and flavor-enhancing properties. Traditional methods of obtaining these compounds, such as extraction from natural sources or chemical synthesis, present challenges related to cost and toxicity, respectively. Enzymatic synthesis, particularly using immobilized lipases, offers a sustainable and efficient alternative. This study investigates the application of CRL immobilized on Diaion HP-20 for geranyl butyrate synthesis via esterification of geraniol and butanoic acid using Candida rugosa lipase (CRL) immobilized on Diaion HP-20 (CRL-DHP-20). The immobilization process resulted in a protein loading of 29.6 ± 2.2 mg/g support from an initial 40 mg/g, and the immobilized biocatalyst exhibited a hydrolytic activity of 124.0 ± 2.5 U/g using olive oil emulsion. Reaction conditions were optimized through a central composite design, evaluating the influence of biocatalyst concentration, temperature, and agitation on ester conversion. The optimal conditions (13.4% CRL-DHP-20, 48.2 °C, and 220.1 rpm) led to 85.4% conversion in 360 min. Additionally, CRL-DHP-20 retained 84% of its initial activity after six reaction cycles, indicating good operational stability. These findings highlight the potential of CRL-DHP-20 as an effective and reusable biocatalyst for green synthesis of flavor esters.
20 June 2026







