Virgen-Ortiz, Jose J., Santos, Jose Cleiton S. dos, Ortiz, Claudia, Berenguer-Murcia, Ángel, Barbosa, Oveimar, Rodrigues, Rafael C., Fernández Lafuente, Roberto
Lecitase ultra: A phospholipase with great potential in biocatalysis
Molecular Catalysis. 2019, 473: 110405. doi:10.1016/j.mcat.2019.110405
URI: http://hdl.handle.net/10045/92515
DOI: 10.1016/j.mcat.2019.110405
ISSN: 2468-8231
Abstract: 
Lecitase Ultra is a chimera produced by the fusion of the genes of the lipase from Thermomyces lanuginosus and the phospholipase A1 from Fusarium oxysporum. The enzyme was first designed for the enzymatic degumming of oils, as that problem was not fully resolved before. It is commercialized only as an enzyme solution by Novo Nordisk A/S. This review shows the main uses of this promising enzyme. Starting from the original degumming use, the enzyme has found applications in many other food modification applications, like production of structured phospholipids (e.g., derivatives of phosphatidylcholine), tuning the properties of flour, etc. Moreover, the enzyme has been used in fine chemistry (resolution of racemic mixtures), in the production of aromas and fragrances, polymers modification, etc. Some papers show the use of the enzyme in biodiesel production. Moreover, we present the different technologies applied to obtain a suitable immobilized biocatalyst, remarking the immobilization via interfacial activation and how heterofunctional acyl supports may solve some of the limitations. Immobilized enzyme physical and chemical modifications have also been presented. Finally, Lecitase Ultra has been one of the model enzymes in a new strategy to coimmobilize lipases and other less stable enzymes.
Keywords:Phospholipase, Oil degumming, Structured lipids, Enzyme immobilization, Interfacial activation, Enzyme stabilization, Enzyme modulation
Elsevier
info:eu-repo/semantics/article