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Merck

Screening of food grade lipases to be used in esterification and interesterification reactions of industrial interest.

Applied biochemistry and biotechnology (2009-03-06)
Ariela Veloso de Paula, Gisele Fátima Morais Nunes, Josiane de Lourdes Silva, Heizir Ferreira de Castro, Júlio César dos Santos
RESUMEN

Seven food grade commercially available lipases were immobilized by covalent binding on polysiloxane-polyvinyl alcohol (POS-PVA) hybrid composite and screened to mediate reactions of industrial interest. The synthesis of butyl butyrate and the interesterification of tripalmitin with triolein were chosen as model reactions. The highest esterification activity (240.63 microM/g min) was achieved by Candida rugosa lipase, while the highest interesterification yield (31%, in 72 h) was achieved by lipase from Rhizopus oryzae, with the production of about 15 mM of the triglycerides C(50) and C(52). This lipase also showed a good performance in butyl butyrate synthesis, with an esterification activity of 171.14 microM/g min. The results demonstrated the feasibility of using lipases from C. rugosa for esterification and R. oryzae lipase for both esterification and interesterification reactions.

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Sigma-Aldrich
Butyl butyrate, 98%
Sigma-Aldrich
Butyl butyrate, ≥98%, FCC, FG
Sigma-Aldrich
Butyl butyrate, natural, ≥98%, FCC, FG