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• W4310588768 abstract "d-Allulose is a desirable sucrose substitute with potential applications in food and health care. d-Allulose can be synthesized using d-glucose as a substrate through coupling glucose isomerase with d-allulose 3-epimerase (DAEase); however, the product yield is typically less than 20% at reaction equilibrium and thus limits its use in industrial applications. Here, a 3R-ketose phosphorylation pathway coupled with an adenosine triphosphate (ATP) regeneration system was developed for the efficient synthesis of d-allulose in Escherichia coli using d-glucose as a substrate. The l-rhamnulose kinase (RhaB) was used to break the inherent reaction equilibrium due to its substrate specificity, resulting in increases in d-allulose titer by 69.9% to 4.96 ± 0.49 g/L. By optimizing the whole cell transformation conditions and designing an ATP regeneration module, d-allulose production reached 17.62 ± 0.77 g/L from 30 g/L d-glucose with a final yield of 0.73 g/g without the addition of exogenous ATP. To evaluate the potential industrial application of this multienzyme cascade system, d-allulose was produced from cane molasses (124.16 ± 2.69 g/L glucose equivalent) with a final d-allulose titer of 62.60 ± 3.76 g/L. The present study provides a practical enzymatic approach for the economical synthesis of d-allulose." @default.
• W4310588768 created "2022-12-12" @default.
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• W4310588768 date "2022-12-02" @default.
• W4310588768 modified "2023-10-18" @default.
• W4310588768 title "Phosphorylation-Driven Production of <scp>d</scp>-Allulose from <scp>d</scp>-Glucose by Coupling with an ATP Regeneration System" @default.
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• W4310588768 doi "https://doi.org/10.1021/acs.jafc.2c06920" @default.
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