Applications of immobilized Thermomyces lanuginosa lipase in interesterification

Abstract

The aim of this work was to investigate the catalytic functions of a new immobilized Thermomyces lanuginosa lipase in interesterification and to optimize the conditions of interesterification for the production of human milk fat substitutes (HMFS) containing n-3 PUFA by response surface methodology (RSM). Thermomyces lanuginosa lipase had an activity similar to that of immobilized Rhizomucor miehei lipase (Lipozyme RM IM) in the glycerolysis of sunflower oil, but the former had higher activity at a low reaction temperature (5°C). Thermomyces lanuginosa lipase was found to have much lower catalytic activity than Lipozyme RM IM in the acidolysis of sunflower oil with caprylic acid. However, the activity of T. lanuginosa lipase was only slightly lower than that of Lipozyme RM IM in the ester-ester exchange between tripalmitin (PPP) and the ethyl esters of EPA and DHA (EE). For this reason, the new immobilized T. lanuginosa lipase was used to produce HMFS from PPP by interesterification with EE. The optimization of major parameters was conducted with the assistance of RSM. The optimal conditions generated were a substrate molar ratio of 5 (EE/PPP), a lipase load of 20 wt% (on substrates), and a reaction time of 20 h, with acyl incorporation up to 42%. The model generated significantly represented real relationships between the response (incorporation) and reaction parameters.

Synthesis and Characterization of Phenolic Lipids

“…The choice of the proper substrate molar ratio is also related to the downstream processing expenses and associated diiculties of separating FFAs or acyl donors by evaporation and/or distillation. Previous studies have shown that high substrate molar ratio would require a shorter reaction time, move the reaction equilibrium to the product formation, and improve the acyl incorporation [114,115]. Yang et al [114] reported the positive efect of substrate molar ratio on the interesteriication reaction between EPA and DHA ethyl esters and tripalmitin.…”

“…Previous studies have shown that high substrate molar ratio would require a shorter reaction time, move the reaction equilibrium to the product formation, and improve the acyl incorporation [114,115]. Yang et al [114] reported the positive efect of substrate molar ratio on the interesteriication reaction between EPA and DHA ethyl esters and tripalmitin. They indicated that the optimization results suggested a molar ratio of 6 along with an enzyme load of 20% (Lipozyme TL-IM) and a 17.9 h reaction time would provide the highest incorporation.…”

Lipídios estruturados: alternativa para a produção de sucedâneos da gordura do leite humano

“…13,38,49,73,[78][79][80][81][82][83] Pesquisadores patentearam diferentes métodos de produção de lipídios estruturados e utilização em fórmulas infantis na Europa 84 e na Austrália. 78 Diferentes tipos de óleos e gorduras são utilizados como substratos para a produção de lipídios estruturados sucedâneos da gordura do leite humano, como o tripalmitoilglicerol, gordura suína (banha), gordura do leite bovino, óleo de soja, óleo de canola, óleo de borage e óleo de girassol.…”

“…Yang et al 83 utilizaram as enzimas Lipozyme IM ® TL de Thermomyces lanuginosa para interesterificar o tripalmitoilglicerol com ácido caprílico e óleo de girassol, visando produzir lipídio estruturado semelhante ao lipídio do leite humano. As melhores incorporações de ácido palmítico (42%) foram obtidas nas seguintes condições: 20% de enzima por 20 h de reação a 40 ºC.…”

Enzymatic Interesterification of Soybean Oil and Methyl Stearate Blends Using Lipase Immobilized on Magnetic Fe3O4/SBA-15 Composites as a Biocatalyst

“…Among them, enzyme immobilization is a widely employed method to impart the desirable features of enzymes 14,15 . Immobilized lipase provides important advantages to the process, such as the ease in catalyst recycling, continuous operation, and product purification.…”