EVALUATIONS ON ENZYMATIC EPOXIDATION, EFFICIENCY AND DECAY

• Main Author: Molina, Elena A Robles
• Format: Thesis
• Language: unknown
• Published: Purdue University Graduate School 2020
• Subjects: 90301 Biomaterials; FOS Medical engineering; 91205 Functional Materials; FOS Materials engineering; 91209 Polymers and Plastics; 90608 Renewable Power and Energy Systems Engineering excl. Solar Cells; FOS Electrical engineering, electronic engineering, information engineering; 100302 Bioprocessing, Bioproduction and Bioproducts; FOS Industrial biotechnology; 100301 Biocatalysis and Enzyme Technology; 60107 Enzymes; FOS Biological sciences; Antarc*; Antarctica
• Online Access: https://dx.doi.org/10.25394/pgs.13359929; https://hammer.figshare.com/articles/thesis/EVALUATIONS_ON_ENZYMATIC_EPOXIDATION_EFFICIENCY_AND_DECAY/13359929

The potential use of enzymes in industrial synthesis of epoxidized soybean oil has been limited through the high cost of the enzyme catalyst, in this work we evaluate the effectiveness of chemo enzymatic epoxidation of high oleic soybean oil (HOSBO) using lipase B from Candida antarctica (CALB) on immobilization support Immobead 150 and H 2 O 2 in a solvent-free system. Additionally, we evaluated the production decay rates for hydrolytic activity and epoxide product formation over consecutive batches to determine half-life of the enzyme catalyst. Batch epoxidation of HOSBO using CALB on 4wt% loading shows yields higher than 90% after 12 hrs. of reaction, and with a correlation to the consumption of double bonds suggesting that the reaction is selective and limiting side product reactions. Non-selective hydrolysis of oil was not found beyond the initial hydrolysis degree of raw HOSBO. Evaluations of decay given by epoxide product formation and released free fatty acids shows a half-life of the enzyme catalyst on these activities is of 22 ad 25 hrs. respectively. Finally, we evaluated the physical parameters influencing this decay, and found that H 2 O 2 presence is the most important parameter of enzyme inactivation with no significant effect from its slowed addition. We propose a new reactor configuration for the analysis of the specific steps on epoxide formation through peracid intermediates.