Screening of Lipases with Unusual High Activity in the sn-2 Esterification of 1,3-Dicaprin under Mild Operating Conditions

DANIEL SÁNCHEZ; GABRIELA MARTA TONETTO; MARÍA LUJÁN FERREIRA

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

AMER CHEMICAL SOC

Lugar: Washington; Año: 2017 p. 5010 - 5017

0021-8561

In this work, the synthesis of acylglycerides with high nutritional value was carried out by enzymatic esterificationat sn-2 position of 1,3-dicaprin with palmitic acid. A comparative study of the performance of several biocatalysts according to theobtained products was carried out. The results obtained with several of the biocatalysts evaluated are very interesting, and itwould be possible to use them to obtain a mixture of acylglycerides to act as a fat substitute. The final product was composed ofabout 90% of nutritionally attractive glycerides. These glycerides were medium-chain length triglycerides, medium−long chaintriglycerides (mainly triglycerides with medium chain fatty acids at sn-1 and sn-3 positions and long chain fatty acid at sn-2position), and 1,3-diglycerides. Pseudomonas f luorescens lipase and Burkholderia cepacia lipase immobilized on chitosandemonstrated unusual high activity in the sn-2 esterification of 1,3-dicaprin with palmitic acid at 45 °C and 12 h with 33% yield to1,3-dicaproyl-2-palmitoyl glycerol. Burkholderia cepacia lipase has the advantage of being immobilized; however, BCL/chitosanhas the advantages of being immobilized and therefore its easy recovery from the reaction media.