Applications of immobilized <Emphasis Type="Italic">Thermomyces lanuginosa</Emphasis> lipase in interesterification |
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Authors: | Tiankui?Yang Maj-Britt?Fruekilde Email author" target="_blank">Xuebing?XuEmail author |
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Affiliation: | (1) Food Biotechnology and Engineering, BioCentrum-DTU, Technical University of Denmark, Building 221, DK-2800 Lyngby, Denmark |
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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 assistante 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. |
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Keywords: | Docosahexaenoic acid (DHA) eicosapentaenoic acid (EPA) human milk fat substitutes interesterification Thermomyces lanuginosa lipase tripalmitin |
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