Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 62, Issue 7, Pages 1617-1624Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf404785m
Keywords
L-arabinose isomerase; D-xylose (glucose) isomerase; D-tagatose; D-fructose; food grade; Lactobacillus
Funding
- Austrian Science Fund FWF [P22094]
- Austrian Science Fund (FWF) [P 22094] Funding Source: researchfish
- Austrian Science Fund (FWF) [P22094] Funding Source: Austrian Science Fund (FWF)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available