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Enhanced Promiscuity of Lipase-Inorganic Nanocrystal Composites in the Epoxidation of Fatty Acids in Organic Media.

In the present study, Candida antarctica lipase B (CALB) was encapsulated in inorganic nanocrystal composites with flower-like shapes, retaining 92% of its catalytic activity compared to that of native lipase. Surprisingly, CALB-inorganic crystal nanoflowers exhibited promiscuous activity at levels 25- and 4-fold higher than those of native lipase and the commercial immobilized lipase Novozym 435, respectively, as demonstrated by the chemoenzymatic epoxidation of fatty acids conducted in organic media. To the best of our knowledge, we showed for the first time that the promiscuity of enzymes can be significantly improved by enzyme immobilization, suggesting that the enzyme-inorganic nanocrystal composites are a very promising type of immobilized enzyme that can be used to address the challenge of the extremely low efficiency of enzymatic promiscuity.