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Literature summary for 3.2.1.11 extracted from

  • Ryu, H.; Jin, X.; Lee, J.; Woo, H.; Kim, Y.; Kim, G.; Seo, E.; Kang, H.; Kim, J.; Cho, D.; Kimura, A.; Kim, D.
    Optimal expression and characterization of a fusion enzyme having dextransucrase and dextranase activities (2010), Enzyme Microb. Technol., 47, 212-215.
No PubMed abstract available
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Cloned(Commentary)

Cloned (Comment) Organism
gene dex2, expression of the engineered fusion enzyme DSXR in Escherichia coli strain BL21(DE3)pLysS, optimization of protein expression conditions for enhancement of protein production by the effects of three-level-three-factors and their mutual interaction in Escherichia coli Pseudarthrobacter oxydans

Protein Variants

Protein Variants Comment Organism
additional information generation of an engineered fusion enzyme of dextransucrase, from dsrBCB4 gene from Leuconostoc mesenteroides B-1299CB4, and Arthrobacter oxydans dextranase, i.e. DSXR. DSXR is potentially useful for reliable production of long isomalto-oligosaccharides from sucrose by a one-step reaction Pseudarthrobacter oxydans

Organism

Organism UniProt Comment Textmining
Pseudarthrobacter oxydans A9UKG4 gene dex2
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 activities of recombinant fusion protein and of wild-type dextranase in fermentation, overview Pseudarthrobacter oxydans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
 recombinant wild-type dextranase Pseudarthrobacter oxydans
5.8
-
 recombinant engineered fusion protein DSXR Pseudarthrobacter oxydans

pH Range

pH Minimum pH Maximum Comment Organism
5 6.4 great loss in activity below and above that values, recombinant wild-type dextranase and engineered fusion protein DSXR Pseudarthrobacter oxydans