Abstract
BackgroundSaccharomyces cerevisiae AN120 osw2∆ spores were used as a host with good resistance to unfavorable environment. This work was undertaken to develop a new yeast spore-encapsulation of Candida parapsilosis Glu228Ser/(S)-carbonyl reductase II and Bacillus sp. YX-1 glucose dehydrogenase for efficient chiral synthesis in organic solvents.ResultsThe spore microencapsulation of E228S/SCR II and GDH in S. cerevisiae AN120 osw2∆ catalyzed (R)-phenylethanol in a good yield with an excellent enantioselectivity (up to 99%) within 4 h. It presented good resistance and catalytic functions under extreme temperature and pH conditions. The encapsulation produced several chiral products with over 70% yield and over 99% enantioselectivity in ethyl acetate after being recycled for 4–6 times. It increased substrate concentration over threefold and reduced the reaction time two to threefolds compared to the recombinant Escherichia coli containing E228S and glucose dehydrogenase.ConclusionsThis work first described sustainable enantioselective synthesis without exogenous cofactors in organic solvents using yeast spore-microencapsulation of coupled alcohol dehydrogenases.
Highlights
Saccharomyces cerevisiae AN120 osw2∆ spores were used as a host with good resistance to unfavora‐ ble environment
Co‐encapsulation of E228S/(S)-carbonyl reductase (SCRII) and glucose dehydrogenase (GDH) in spores of S. cerevisiae AN120 osw2Δ It was reported that the Shine-Dalgarno (SD) and aligned spacing (AS) sequence could initiate protein translation efficiently [20]
The co-encapsulation of E228S/SCRII and GDH in S. cerevisiae AN120 osw2Δ was performed by SD-Trp screening as described in “Materials and methods” [18]
Summary
Saccharomyces cerevisiae AN120 osw2∆ spores were used as a host with good resistance to unfavora‐ ble environment. YX-1 glucose dehydrogenase for efficient chiral synthesis in organic solvents. Alcohol dehydrogenases (ADHs) in organic synthesis have attracted particular interest for the improvement of substrate permeability, cofactor regeneration and process simplification [1, 2]. Few ADH exhibited solvent-resistant properties associated with their sustainable enantioselective catalytic functions [3]. Enzyme encapsulation is a practical technique to improve enzyme stability and performance, such as the. To realize efficient enantioselective synthesis, chiral-forming ADH and cofactor-recycling ADH are encapsulated for in situ cofactor regeneration [6, 7]. Liu et al encapsulated glutamate dehydrogenase and lactate dehydrogenase and their cofactor in three nanoparticles, but they performed reaction with low concentrated substrates [8]. El-Zahab et al carried out stereospecific reaction with 10 mM glutamate with particle-tethered NADH shuttled between co-immobilized
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