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• W4382181287 abstract "An enzyme cascade was established previously consisting of a recycling system with an l-amino acid oxidase (hcLAAO4) and a catalase (hCAT) for different α-keto acid co-substrates of (S)-selective amine transaminases (ATAs) in kinetic resolutions of racemic amines. Only 1 mol % of the co-substrate was required and l-amino acids instead of α-keto acids could be applied. However, soluble enzymes cannot be reused easily. Immobilization of hcLAAO4, hCAT and the (S)-selective ATA from Vibrio fluvialis (ATA-Vfl) was addressed here. Immobilization of the enzymes together rather than on separate beads showed higher reaction rates most likely due to fast co-substrate channeling between ATA-Vfl and hcLAAO4 due to their close proximity. Co-immobilization allowed further reduction of the co-substrate amount to 0.1 mol % most likely due to a more efficient H2 O2 -removal caused by the stabilized hCAT and its proximity to hcLAAO4. Finally, the co-immobilized enzyme cascade was reused in 3 cycles of preparative kinetic resolutions to produce (R)-1-PEA with high enantiomeric purity (97.3 %ee). Further recycling was inefficient due to the instability of ATA-Vfl, while hcLAAO4 and hCAT revealed high stability. An engineered ATA-Vfl-8M was used in the co-immobilized enzyme cascade to produce (R)-1-(3-ethoxy-4-methoxyphenyl)-2-(methylsulfonyl)ethanamine, an apremilast-intermediate, with a 1,000 fold lower input of the co-substrate." @default.
• W4382181287 created "2023-06-28" @default.
• W4382181287 creator A5002023732 @default.
• W4382181287 creator A5004420169 @default.
• W4382181287 creator A5019121662 @default.
• W4382181287 creator A5031181844 @default.
• W4382181287 creator A5074716708 @default.
• W4382181287 creator A5077845134 @default.
• W4382181287 creator A5082227921 @default.
• W4382181287 date "2023-08-10" @default.
• W4382181287 modified "2023-10-18" @default.
• W4382181287 title "Co‐Immobilization of a Multi‐Enzyme Cascade: (<i>S</i>)‐Selective Amine Transaminases, <scp>l</scp>‐Amino Acid Oxidase and Catalase" @default.
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