99A-17 |
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J. A. NORIEGA-RODRÍGUEZ1, N. Gamez-Meza2, J. Ortega-Garcia2, L. A. Medina-Juárez3, and H. S. Garcia4. (1) Departamento de Investigaciones Cientificas y Tecnologicas, Universidad de Sonora, Rosales y Niños Heroes s/n col. Centro., 83000 Hermosillo, 83000, Mexico, (2) DICTUS, Universidad de Sonora, Rosales y Niños Heroes s/n col. centro, 83000 Hermosillo, 83000, Mexico, (3) Departamento de Investigaciones Científicas y Tecnológicas, Universidad de Sonora, Rosales y Noños Heroes, 83000 Hermosillo, 83000, Mexico, (4) UNIDA, Instituto Tecnologico de Veracruz, M.A. de Quevedo # 2779, Col. Formando Hogar, Veracruz, Ver., 91897, Mexico Enzymatic hydrolysis has been widely studied for the production of n-3 polyunsaturated fatty acid (n-3 PUFA) concentrates. However, there is a lack of information about the kinetic parameters for the esterification of n-3 PUFA. The activity and specificity that commercial enzymes present for the hydrolysis are different for the esterification. In this work the activity and specificity of commercial lipases for the esterification of n-3 PUFA from sardine oil in a free solvent media were evaluated. The concentrated of n-3 PUFA was obtained by Chemical hydrolysis from the sardine oil followed by urea-complexation. Three Inmoblilized lipases from Pseudomonas cepacia (PS-C Amano I and PS-C Amano II on celita; PS-D Amano I on diatomea earths), one from Candida antarctica (Novozym 435 on mocroporous acrylic resin); and three soluble enzymes AK20 from Pseudomonas sp., A12 from Aspergillus níger, and FAP-15 from Rhizopus oryzae; were screened for the esterification of n-3 PUFA to glycerol. The initial velocity was obtained using a deactivation extended first order model and the Michaellis-Menten parameters for the different substrate concentration were determined. Results show that all enzymes were able to esterified the n-3 PUFA to glycerol but with different activity. Enzymes from Pseudomonas cepacia exhibited the lowest esterifcation degree (3-20% after 12 h), soluble enzymes produced 45-55% and Novozym 435 reach 90.82% of esterification in a 4 h reaction period. The kinetic parameters for the esterification of eicosapentaenoic acid (Vmax=0.0350 mmol/mol h; Km=0.0724 mol glycerol/mol FFA) and docosahexaenoic acid (Vmax=0.0717 mmol/mol h; Km=0.1177 mol glycerol/mol FFA) with Novozym 435 were obtained and global esterification exhibit a Ea=25.91 kJ/mol. The results and parameters obtained on this work can be useful for the design of a industrial process for the production of glycerides with a high concentration of n-3 PUFA.
Session 99A, Biotechnology: General
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