Pseudomonas stutzeri lipase

Hoyos, P., Buthe, A., Ansorge-Schumacher, M.B. et al. (2008) Highly efficient one pot dynamic kinetic resolution of benzoins with entrapped Pseudomonas stutzeri lipase. Journal of Molecular Catalysis B, Enzymatic, 52-53,133-139. 

In 2006, Alcantara s group reported the first DKR of different benzoins by using Pseudomonas stutzeri lipase (lipase TL) and Shvo s catalyst in organic solvents, obtaining the corresponding (5)-acylated products with yields of up to 87% and enantioselectivities of >99% ee (Scheme 4.21). In all cases, the particular stereobias of the lipase towards the racemic substrates allowed the production of the opposite enantiomer to that prepared through a different enzymatic methodology. 

An efficient DKR protocol for benzoins (l,2-diaryl-2-hydroxyethanones) was presented by Alcantara and coworkers in 2006 using Shvo s catalyst 1 for the racemization [78]. For the enzymatic resolution, Pseudomonas stutzeri lipase (Lipase TL) was used, giving the (5 )-acylated products in excellent enantiomeric excesses (>99% ee) and with yields up to 90% (16). The chiral benzoins have synthetic importance as building blocks for different heterocycles. 

Pseudomonas stutzeri lipase CAL-B, SCCO2 TL lipase, acetone, isopropenyl acetate VinOAc, 20 °C, 24 h VinOAc, 45 °C, 95 min 37 °C, 18 h... 

DKR with lipase TL (from Pseudomonas stutzeri) was part of the reaction scheme in work reported by Hoyos et al. [24]. Here the lipase is immobilized using a number of... 

Maraite, A., Hoyos, R, Daniel Garballeira, J., Cabrera, A. C., et al. (2013). Lipase from Pseudomonas stutzeri Rurification, homology modelling and rational explanation of the substrate binding mode.. Mol. Catal. B Enzym., 87,88-98. 

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