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Operational stability of Thermomyces lanuginosa lipase during interesterification of fat in continuous packed‐bed reactors
Author(s) -
Osório Natália M.,
da Fonseca M. Manuela R.,
FerreiraDias Suzana
Publication year - 2006
Publication title -
european journal of lipid science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 94
eISSN - 1438-9312
pISSN - 1438-7697
DOI - 10.1002/ejlt.200600029
Subject(s) - interesterified fat , lipase , chemistry , palm stearin , sunflower oil , packed bed , chromatography , bioreactor , triacylglycerol lipase , food science , organic chemistry , palm oil , enzyme
The operational stability of a commercial immobilized lipase from Thermomyces lanuginosa (“Lipozyme TL IM”) during the interesterification of two fat blends, in solvent‐free media, in a continuous packed‐bed reactor, was investigated. Blend A was a mixture of palm stearin (POS), palm kernel oil (PK) and sunflower oil (55 : 25 : 20, wt‐%) and blend B was formed by POS, PK and a concentrate of triacylglycerols rich in n ‐3 polyunsaturated fatty acids (PUFA) (55 : 35 : 10, wt‐%). The bioreactor operated continuously at 70 °C, for 580 h (blend A) and 390 h (blend B), at a residence time of 15 min. Biocatalyst activity was evaluated in terms of the decrease of the solid fat content at 35 °C of the blends, which is a key parameter in margarine manufacture. The inactivation profile of the biocatalyst could be well described by the first‐order deactivation model: Half‐lives of 135 h and 77 h were estimated when fat blends A and B, respectively, were used. Higher levels of PUFA in blend B, which are rather prone to oxidation, may explain the lower lipase stability when this mixture was used. The free fatty acid content of the interesterified blends decreased to about 1% during the first day of operation, remaining constant thereafter.