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Enzyme–Support Interactions of Burkholderia cepacia Lipase Immobilized on Silica Using Molecular Docking and Multitechnique Characterization
Introduction Click to copy section linkSection link copied! Immobilized lipases have gained increasing attention as alternatives to free enzymes, primarily due to their ability to retain enzymatic activity postimmobilization. However, understanding the underlying causes of specific activity variations remains challenging due to the numerous contributing factors. (1) This lack of knowledge hinders the design and understanding at the molecular level of the bottlenecks in the immobilization process.
Biocatalytic Production of Solketal Esters from Used Oil Utilizing Treated Macauba Epicarp Particles as Lipase Immobilization Support: A Dual Valorization of Wastes for Sustainable Chemistry
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Production of Human Milk Fat Substitutes by Lipase-Catalyzed Acidolysis: Immobilization, Synthesis, Molecular Docking and Optimization Studies
2.4. Optimization of the Enzymatic Acidolysis In order to develop an acidolysis process with a high yield for the oleic acid incorporation, the influence of reaction temperature (T) and molar ratio (MR) were evaluated. The enzyme loading in the support was maintained constant at 5% (w/w of tripalmitin) according to the amount used in similar studies [14,15,31]. The results of the set of 11 experiments of the CCRD are presented in Table 1.
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