Mutated variant of Candida antarcticalipase B in (S)-selective dynamic kinetic resolution of secondary alcohols

Abstract

An (S)-selective dynamic kinetic resolution of secondary alcohols, employing a mutated variant of Candida antarctica lipase B (CalB) gave products in 84-88% yield and in 90-97% ee.

A general protein purification and immobilization method on controlled porosity glass: biocatalytic applications

“…[26][27][28] This enzyme was readily bound to EziG™ within 30 min of incubation while ten days of incubation was required for immobilization on Accurel®. For this variant, EziG™ (HybCPG VBC) is a more suitable carrier than Accurel® based on the bulk volumetric activity and the time needed for immobilization (see Table S2, Supplementary Information).…”

Lipases: Valuable catalysts for dynamic kinetic resolutions

“…Several complexes of Ru (II) have been combined with lipases for DKR of alcohols, some of which are depicted in Fig. 8 (Agrawal et al, 2014;Akai et al, 2004;Benaissi et al, 2009;Bogár and Bäckvall, 2007;Bogár et al, 2007aBogár et al, , 2007bChen and Yuan, 2010;Choi et al, 2002Choi et al, , 2004Csjernyik et al, 2004;Das and Nanda, 2012;Do et al, 2010;Edin et al, 2006;Ema et al, 2012;Engstrom et al, 2011;Fransson et al, 2006;Hilker et al, 2006;Johnston et al, 2010;Kim et al, 2003Kim et al, , 2004Kim et al, , 2005Kim et al, , 2008H. Kim et al, 2011;C.…”

“…Catalyst 4 is particularly one of the most efficient Ru (II) complexes used for racemization in chemoenzymatic dynamic kinetic resolutions (Csjernyik et al, 2004;Martín-Matute et al, 2004. This catalyst is activated by bases such as t-BuOK and is able to quickly racemize alcohols under mild temperatures in the presence of lipases, so that it has been employed in the DKR of several alcohols Bogár et al, 2007aBogár et al, , 2007bCsjernyik et al, 2004;Edin et al, 2006;Ema et al, 2012;Engstrom et al, 2011;Fransson et al, 2006;Johnston et al, 2010;S. Kim et al, 2013;Krumlinde et al, 2009;Leijondahl et al, 2009;Lihammar et al, 2011Lihammar et al, , 2013Mangas-Sánchez et al, 2009;Martín-Matute et al, 2004, 2006Norinder et al, 2007;Shuklov et al, 2014;Solarte et al, 2014;Träff et al, 2008Träff et al, , 2011Warner et al, 2012), including the large-scale DKR of 1-phenylethanol to give (R)-1-phenylethanol (Bogár et al, 2007a).…”

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

“…Thus, Bäckvall and co-workers have applied CAL-B mutants to access to a series of (S)-acetate products with excellent conversions and ee when combined with Ru-complex 2, inverting the selectivity displayed by the wild-type enzyme. [39] A similar approach described by Ema et al. allowed the successful deracemization via DKR of several sterically hindered secondary alcohols using a mutant of lipase from Burkholderia (Pseudomonas) cepacia together with 2 to synthesize the corresponding (R)-esters in high yields (>70%) and excellent selectivities (>95%).…”