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Gewählte Publikation:

Staudigl, P; Haltrich, D; Peterbauer, CK.
(2014): L-Arabinose Isomerase and D-Xylose Isomerase from Lactobacillus reuteri: Characterization, Coexpression in the Food Grade Host Lactobacillus plantarum, and Application in the Conversion of D-Galactose and D-Glucose
J AGR FOOD CHEM. 2014; 62(7): 1617-1624. FullText FullText_BOKU

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 degrees C and pH 6.0, whereas D-XI showed maximum activity at 65 degrees 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 degrees C.
Autor*innen der BOKU Wien:
Haltrich Dietmar
Peterbauer Clemens Karl
Staudigl Petra

Find related publications in this database (Keywords)
L-arabinose isomerase
D-xylose (glucose) isomerase
food grade

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