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Literature summary for 4.2.2.16 extracted from

  • Lim, S.; Lee, K.Y.; Lee, Y.B.; Song, K.B.
    Immobilization of levan fructotransferase for the production of di-fructose anhydride from levan (2001), Biotechnol. Lett., 23, 1335-1339.
No PubMed abstract available
Search for more literature for 4.2.2.16

General Stability

General Stability Organism
enzyme immobilized on Chitopearl BCW2501 beads retains about 60% of its initial activity after being used for 20 cycles Paenarthrobacter ureafaciens

Organism

Organism UniProt Comment Textmining
Paenarthrobacter ureafaciens
-
-
-
Paenarthrobacter ureafaciens K2032
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
levan
-
 Paenarthrobacter ureafaciens 5 di-D-fructose-2,6':2',6 dianhydride + ?
-
 ?
levan
-
 Paenarthrobacter ureafaciens K2032 5 di-D-fructose-2,6':2',6 dianhydride + ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
 free enzyme Paenarthrobacter ureafaciens
60
-
 enzyme immobilized on Chitopearl BCW2501 Paenarthrobacter ureafaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 60 min, 45% loss of activity of enzyme immobilized on Chitopearl BCW2501 beads, 95% loss of activity of native enzyme. Native enzyme loses about 80% of its initial activity after 30 min Paenarthrobacter ureafaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
 enzyme immobilized to Diaion WA30 Paenarthrobacter ureafaciens
4 5.5 enzyme immobilized on Chitopearl BCW2501 beads Paenarthrobacter ureafaciens
6
-
 free enzyme Paenarthrobacter ureafaciens