کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2716 | 127 | 2016 | 7 صفحه PDF | دانلود رایگان |
• 4 immobilized enzymes transform racemic esters into prochiral ketones.
• The immobilized biocatalysts allow the regeneration of NAD+ with a TOF of 294 h−1.
• The immobilized enzymatic consortium is stable under 10 operational cycles.
One-pot multi-step conversions are desirable to achieve more efficient and sustainable chemical processes. In this context, the immobilization of multi-enzyme systems allows the reusability of several stabilized biocatalysts working in cascade and orthogonal reactions to access more complex synthetic schemes. Herein, we have shown the one-pot tandem hydrolysis and oxidation of racemic esters (1-phenylethyl acetate) to yield quantitative conversion of prochiral ketones (acetophenone) catalyzed by a consortium of immobilized enzymes. Eukaryotic lipase and catalase, and microbial thermophilic alcohol dehydrogenase and NADH oxidase are covalently, irreversibly and individually immobilized onto four different carriers, achieving high immobilization yields (>95%) for all the enzymes, and residual activities >50% for both thermophilic alcohol dehydrogenase and NADH oxidase, 18% for the catalase and 10% for the lipase. This heterogeneous system efficiently recycles NAD+ with a maximum turnover frequency (TOF) of 294 h−1 and can be reused for up to 10 operational cycles, retaining more than 80% of its initial activity.
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Journal: Biochemical Engineering Journal - Volume 112, 15 August 2016, Pages 136–142