Enzyme catalytic promiscuity: asymmetric aldol addition reaction catalyzed by a novel thermophilic esterase in organic solvent

Abstract

The asymmetric aldol addition of 2-butanone and 4-nitrobenzaldehyde catalyzed by a novel thermophilic esterase (APE1547) from the archaeon Aeropyrum pernix K1 was successfully conducted in organic solvents. APE1547 exhibited a good enzyme activity and enantioselectivity in the reaction. The effects of organic solvent, temperature, water content, and substrate concentration were investigated. The reaction provided optically active secondary alcohol with satisfying enantioselectivity (71.2 %ee) and enzyme activity (38.1 µmol/g/h) under the optimum conditions. A high yield (68.7%) could be obtained when the reaction time was approximately 120 h.

Recent Advances in Biocatalytic Promiscuity: Hydrolase‐Catalyzed Reactions for Nonconventional Transformations

“…Leaving aside the proteases, a novel thermophilic esterase (APE1547) from the archaeon Aeropyrum pernix K1 has been reported to catalyze the asymmetric aldol addition of 2‐butanone and 4‐nitrobenzaldehyde in organic solvents . The effects of organic solvent, temperature, water content and substrate concentration were investigated, leading to the corresponding ( S )‐product in approximately 69% yield and 71% ee after 120 h at 65°C.…”

A Simple Screening and Optimization Bioprocess for Long-Chain Peptide Catalysts Applied to Asymmetric Aldol Reaction

“…The asymmetric aldol reaction plays a pivotal role in constructing the C-C bond of chiral alcohols in a single step [3]. A variety of catalysts have been reported in relation to the asymmetric aldol reaction, including metals [4], enzymes [5,6], catalytic antibodies [7,8], and small molecules (also known as organocatalysts) [9][10][11][12]. For instance, in 2007, Inoue reported that chiral bis(oxazolinyl)phenyl-rhodium complexes served as catalysts in the coupling of AgOTf for the direct aldol reaction of ketones and aromatic aldehydes, resulting in the formation of corresponding β-hydroxyketones with high antiselectivity and high enantioselectivity with an up to 91% enantiomeric excess (ee) value.…”

Reações aldólicas em biocatálise: o emprego de lipases como catalisadores e a aplicação do meio reacional de miniemulsão

“…Ainda no que se referem às hidrolases (lipases, proteases e esterases), a protease alcalina de Bacillus licheniformis (BLAP) foi empregada em reações aldólicas entre aldeídos aromáticos e cetonas cíclicas em meio orgânico na presença de água . Assim como a protease ácida de Aspergillus usamii (AUP) (Xie et al, 2012), a chimopapaina (CHI) (He et al, 2012), a tripsina (TRIP) (Chen et al, 2013), a ficina (FIC) (Fu et al, 2013), a proteinase de Aspergillus melleus (AMP) (Yuan et al, 2013), a Nuclease P1 de Penicillium citrinum (NUC) , a esterase termofílica APE1547 em altas temperaturas (50-80 °C) (Haoran et al, 2014) e a esterase de Sulfolobus tokodaii (STE) (Li et al, 2015)…”