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Literature summary for 2.4.1.19 extracted from

  • Moriwaki, C.; Ferreira, L.; Rodella, J.; Matioli, G.
    A novel cyclodextrin glycosyltransferase from Bacillus sphaericus strain 41: production, characterization and catalytic properties (2009), Biochem. Eng. J., 48, 124-131.
No PubMed abstract available

Application

Application Comment Organism
synthesis CGTase is an important industrial enzyme, unique in its capacity to convert starch and related substrates into cyclodextrins through cyclization, an intramolecular transglycosylation reaction Lysinibacillus sphaericus

Inhibitors

Inhibitors Comment Organism Structure
beta-cyclodextrin strong product inhibition of CGTase Lysinibacillus sphaericus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, overview Lysinibacillus sphaericus
0.8
-
maltodextrin pH 6.0, 65°C Lysinibacillus sphaericus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Lysinibacillus sphaericus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
x * 59000, SDS-PAGE Lysinibacillus sphaericus

Organism

Organism UniProt Comment Textmining
Lysinibacillus sphaericus
-
alkalophilic strain 41, isolated from soybean-soil culture
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 315fold by ammonium sulfate fractionation, beta-cyclodextrin affinity chromatography, and ultrafiltration Lysinibacillus sphaericus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
23.5
-
coupling activity, purified enzyme Lysinibacillus sphaericus
75.8
-
cyclization activity, purified enzyme Lysinibacillus sphaericus
198.6
-
disproportionation activity, purified enzyme Lysinibacillus sphaericus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methanol + maltodextrin
-
Lysinibacillus sphaericus alpha-methyl-D-glucopyranoside + beta-cyclodextrin
-
?
additional information in addition to the intramolecular transglycosylation and cyclization producing beta-cyclodextrins, using maltodextrin and starch as substrates, the CGTase shows disproportionation and coupling activities, intermolecular transglycosylation reactions. The enzyme produces alpha-, beta-, and gamma-cyclodextrins in the ratio of 0.40:1:0.45. Activity with different starch types, overview Lysinibacillus sphaericus ?
-
?

Subunits

Subunits Comment Organism
? x * 59000, SDS-PAGE Lysinibacillus sphaericus

Synonyms

Synonyms Comment Organism
CGTase
-
Lysinibacillus sphaericus
cyclodextrin glycosyltransferase
-
Lysinibacillus sphaericus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
cyclization activity Lysinibacillus sphaericus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
35 80 activity range, about 35% of maximal activity at 35°C and 80°C Lysinibacillus sphaericus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35 65 purified native enzyme, 80% remaining activity at 35-65°C, pH 8.0, after 4 h, thermal deactivation above 70°C Lysinibacillus sphaericus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
cyclization activity Lysinibacillus sphaericus

pH Range

pH Minimum pH Maximum Comment Organism
4.5 10 activity range, about 20% of maximal activity at pH 4.5, and 40% at pH 10.0 Lysinibacillus sphaericus

pH Stability

pH Stability pH Stability Maximum Comment Organism
5
-
purified native enzyme, 50°C, 4 h, 34.2% retaining activity Lysinibacillus sphaericus
6 7 purified native enzyme, 50°C, 4 h, almost completely stable Lysinibacillus sphaericus
8 10 purified native enzyme, 50°C, 4 h, 16.8% retaining activity Lysinibacillus sphaericus