Lipases: Valuable catalysts for dynamic kinetic resolutions

• Published in: Biotechnology advances Vol. 33; no. 5; pp. 372 - 393
• Main Authors: de Miranda, Amanda S., Miranda, Leandro S.M., de Souza, Rodrigo O.M.A.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.09.2015
• Subjects: Amines; Biocatalysis; Biotechnology; Catalysis; Chemoenzymatic synthesis; Dynamic kinetic resolution; Dynamics; Enantiomers; Enantioselectivity; Enzyme catalysis; Formations; Kinetics; Lipase; Lipases; Racemization; Reaction kinetics; Stereoisomerism; RT; Enantioselectivity; Racemization; AP-SiO2; PPL; Lipases; MPS; THF; Chemoenzymatic synthesis; Enzyme catalysis; AmP-MCF; NOV435; TBME; DSR; DMP; KR; AIBN; BCL; DKR; Dynamic kinetic resolution; CAL-A; CAL-B; NMM; ISCBCL; MCF; TBAF; Bz; DDKR; IPA; TMS; CRL
• ISSN: 0734-9750; 1873-1899
• DOI: 10.1016/j.biotechadv.2015.02.015

Dynamic kinetic resolutions have proven to be a useful method for the preparation of enantiopure compounds from racemates, leading to the formation of a single enantiomer in theoretically 100% yield. Because lipases are ubiquitous, versatile, stereoselective and robust biocatalysts, they have been successfully applied as co-catalysts in these reactions, being mostly combined with metals in the chemoenzymatic dynamic kinetic resolutions of alcohols and amines. [Display omitted] •Dynamic kinetic resolution is an efficient method for preparation of optically pure compounds•Lipases can be combined with metal-based catalysts in dynamic kinetic resolutions of alcohols and amines•Lipases have been applied in dynamic kinetic resolution of substrates whose racemization is feasible without metal catalysts•Biocatalysts can also be useful as racemization catalysts in dynamic kinetic resolution