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Literature summary extracted from

  • Zhekova, B.; Pishtiyski, I.; Stanchev, V.
    Investigation on cyclodextrin production with cyclodextrin glucanotransferase from Bacillus megaterium (2008), Food Technol. Biotechnol., 46, 328-334.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.19 Cyclodextrins the enzyme activity is strongly inhibited by the reaction products Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.19 additional information
-
 additional information dynamics of beta-cyclodextrin production, kinetics, overview Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.19 Priestia megaterium
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.19 additional information the enzyme produces alpha-, beta-, and gamma-cyclodextrins from starch, product ratios depend on the duration of the process. The enzyme also shows coupling activity and is able to degrade high concentrations of beta-cyclodextrin and to transform different types of cyclodextrins one into another. Native corn starch and soluble potato starch as substrates, product determination by thin layer chromatography Priestia megaterium ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.19 CGTase
-
 Priestia megaterium
2.4.1.19 cyclodextrin glucanotransferase
-
 Priestia megaterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.19 45
-
 assay at Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.19 7
-
 assay at Priestia megaterium