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- W2033378635 abstract "The l-arabinose isomerase (l-AI) and the d-xylose isomerase (d-XI) encoding genes from Lactobacillus reuteri (DSMZ 17509) were cloned and overexpressed in Escherichia coli BL21 (DE3). The proteins were purified to homogeneity by one-step affinity chromatography and characterized biochemically. l-AI displayed maximum activity at 65 °C and pH 6.0, whereas d-XI showed maximum activity at 65 °C and pH 5.0. Both enzymes require divalent metal ions. The genes were also ligated into the inducible lactobacillal expression vectors pSIP409 and pSIP609, the latter containing a food grade auxotrophy marker instead of an antibiotic resistance marker, and the l-AI- and d-XI-encoding sequences/genes were coexpressed in the food grade host Lactobacillus plantarum. The recombinant enzymes were tested for applications in carbohydrate conversion reactions of industrial relevance. The purified l-AI converted d-galactose to d-tagatose with a maximum conversion rate of 35%, and the d-XI isomerized d-glucose to d-fructose with a maximum conversion rate of 48% at 60 °C." @default.
- W2033378635 created "2016-06-24" @default.
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- W2033378635 date "2014-02-04" @default.
- W2033378635 modified "2023-09-26" @default.
- W2033378635 title "<scp>l</scp>-Arabinose Isomerase and <scp>d</scp>-Xylose Isomerase from <i>Lactobacillus reuteri</i>: Characterization, Coexpression in the Food Grade Host <i>Lactobacillus plantarum</i>, and Application in the Conversion of <scp>d</scp>-Galactose and <scp>d</scp>-Glucose" @default.
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- W2033378635 doi "https://doi.org/10.1021/jf404785m" @default.
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