Gotor-Fernandez V.,University of Oviedo |
Diaz-Rodriguez A.,University of Oviedo |
Lavandera I.,University of Oviedo |
Kanbak-Aksu S.,CLEA Technologies |
And 2 more authors.
Advanced Synthesis and Catalysis | Year: 2012
An efficient catalytic system to oxidize quantitatively aliphatic diols using Trametes versicolor laccase and TEMPO has been developed in aqueous medium. Oxidations have occurred in a non-stereoselective fashion but with complete regio- and/or monoselectivity, obtaining lactones with excellent purity after simple extraction. This catalytic system has been demonstrated to be scalable, compatible with the presence of a variety of functionalities, and also allowed the successful enzyme recycling using a laccase-cross-linked enzyme aggregates (CLEA) preparation. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Source
Van Pelt S.,CLEA Technologies |
Teeuwen R.L.M.,CLEA Technologies |
Janssen M.H.A.,CLEA Technologies |
Sheldon R.A.,CLEA Technologies |
And 5 more authors.
Green Chemistry | Year: 2011
The use of Pseudomonas stutzeri lipase (PSL) as a biocatalyst for aminolysis reactions with bulky substrates has been investigated. PSL compared favorably to Novozym ® 435 (immobilized Candida antarctica lipase B, NOV435) in the aminolysis of various bulky methyl esters and amines. While NOV435 demonstrated a higher rate of aminolysis with methyl 2-phenylpropionic acid as the acyl donor, PSL outperformed NOV435 with secondary amines as the nucleophile. Methanol inhibition and a low affinity for bulky acyl donors were found to be the two main reasons for relatively low rates in the PSL-catalyzed aminolysis reactions. It was demonstrated that the use of molsieve 4A had a significant effect on the aminolysis rate and amide yield, since it enabled the effective removal of the inhibiting methanol from the reaction mixture. © 2011 The Royal Society of Chemistry. Source