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Literature summary for 2.4.1.10 extracted from

  • El-Refai, H.; Abdel-Fattah, A.; Mostafa, F.
    Enzymic synthesis of levan and fructo-oligosaccharides by Bacillus circulans and improvement of levansucrase stability by carbohydrate coupling (2009), World J. Microbiol. Biotechnol., 25, 821-827.
No PubMed abstract available
Search for more literature for 2.4.1.10

Protein Variants

Protein Variants Comment Organism
additional information formation of enzyme-polysaccharide conjugates at 4°C, variations of activity retained of the glycosylated levansucrase are affected by the carbohydrate residue, which is covalently linked to the enzyme molecule, dextran conjugates show highest, pectin conjugates lowest activity. In general, the glycosylated enzyme retains 25-57% of the original specific activity of the free enzyme Niallia circulans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Niallia circulans levan, a polymer of fructose linked by fructofurano side bonds, is produced by the transfructosylation reaction of levansucrase ?
-
 ?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside Niallia circulans
-
 D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
 ?

Organism

Organism UniProt Comment Textmining
Niallia circulans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme from cell culture supernatant by ethanol precipitation with 50% v/v ethanol Niallia circulans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
593
-
 partially purified native enzyme Niallia circulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information levan, a polymer of fructose linked by fructofurano side bonds, is produced by the transfructosylation reaction of levansucrase Niallia circulans ?
-
 ?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside
-
 Niallia circulans D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
 ?
sucrose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n alpha-D-glucopyranoside the highest product molecular weight of 38 kDa is reached at 30°C, and gradually decreases at higher temperatures Niallia circulans D-glucose + beta-D-fructofuranosyl-[(2,6)beta-D-fructofuranosyl-]n+1 alpha-D-glucopyranoside
-
 ?

Synonyms

Synonyms Comment Organism
beta-2,6-fructan: D-glucose-1-fructosyltransferase
-
 Niallia circulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35 40 free, unmodified enzyme Niallia circulans
40
-
 polysaccharide-conjugated enzyme Niallia circulans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 50 activity range, activity profiles of free, unmodified and polysaccharide-conjugated enzymes, overview Niallia circulans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 partially purified enzyme conjugated with different polysaccharides, 1 h. The glycosylated enzyme retains 25-57% of the original specific activity of the free enzyme dependent on the sugar conjugate type, overview Niallia circulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
-
 Niallia circulans

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.4 6.8 activity range, activity profiles of free, unmodified and polysaccharide-conjugated enzymes, overview. Highest, complete stability of both at pH 5.2-5.6 Niallia circulans