Production of human milk fat substitutes enriched in omega-3 polyunsaturated fatty acids using immobilized commercial lipases and Candida parapsilosis lipase/acyltransferase

• Main Authors: Tecelão, Carla, Silva, Joana, Dubreucq, Eric, Ribeiro, Maria H., Ferreira-Dias, Suzana
• Other Authors: Instituto Superior de Agronomia, CEER, Biosystems Engineering, University of Lisbon, Instituto Politécnico de Leiria, Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)
• Format: Conference Object
• Language: English
• Published: HAL CCSD 2009
• Subjects: LIPASE; HUMAN MILK FAT SUBSTITUTES; OMEGA-3 POLYUNSATURATED FATTY ACIDS; OPERATIONAL STABILITY; STRUCTURED LIPIDS; SUCCEDANE DE LAIT; STABILITE OPERATIONNELLE; [CHIM.CATA]Chemical Sciences/Catalysis; Antarc*; Antarctica
• Online Access: https://hal.inrae.fr/hal-02823019

International audience In human milk fat (HMF), palmitic acid (20-30%), the major saturated fatty acid, is mostly esterified at the sn-2 position of triacylglycerols, while unsaturated fatty acids are at the sn-1,3 positions, conversely to that occurring in vegetable oils. This study aims at the production of HMF substitutes by enzyme-catalyzed interesterification of tripalmitin with (i) oleic acid (system I) or (ii) omega-3 polyunsaturated fatty acids (omega-3 PUFA) (system II) in solvent-free media. Interesterification activity and batch operational stability of commercial immobilized lipases from Rhizomucor miehei (Lipozyme RM IM), Thermomyces lanuginosa (Lipozyme TL IM) and Candida antarctica (Novozym 435) from Novozymes, DK, and Candida parapsilosis lipase/acyltransferase immobilized on Accurel MP 1000 were evaluated. After 24-h reaction at 60 °C, molar incorporation of oleic acid was about 27% for all the commercial lipases tested and 9% with C. parapsilosis enzyme. Concerning omega-3 PUFA, the highest incorporations were observed with Novozym 435 (21.6%) and Lipozyme RM IM (20%), in contrast with C. parapsilosis enzyme (8.5%) and Lipozyme TL IM (8.2%). In system I, Lipozyme RM IM maintained its activity for 10 repeated 23-h batches while for Lipozyme TL IM, Novozym 435 and C. parapsilosis enzyme, linear (half-life time, t1/2 = 154 h), series-type (t1/2 = 253 h) and first-order (t1/2 = 34.5 h) deactivations were respectively observed. In system II, Lipozyme RM IM showed linear deactivation (t1/2 = 276 h), while Novozym 435 (t1/2 = 322 h) and C. parapsilosis enzyme (t1/2 = 127 h), presented series-type deactivation. Both activity and stability of the biocatalysts depended on the acyl donor used.