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Literature summary for 2.4.1.19 extracted from

  • Ferrarotti, S.A.; Bolivar, J.M.; Mateo, C.; Wilson, L.; Guisan, J.M.; Fernandez-Lafuente, R.
    Immobilization and stabilization of a cyclodextrin glycosyltransferase by covalent attachment on highly activated glyoxyl-agarose supports (2006), Biotechnol. Prog., 22, 1140-1145.
    View publication on PubMed
Search for more literature for 2.4.1.19

General Stability

General Stability Organism
thermostability at 60°C and pH 7 reveals that the enzyme adsorbed on ionic supports is slightly less stable than the CNBr-agarose immobilized enzyme. The enzyme immobilized on Eupergit presents a very similar stability to this preparation while the glyoxyl-agarose is much more stable than any other preparation (by around a 15-fold factor) the glyoxyl-agarose immobilized enzyme is much more stable than any other preparation in presence of ethanol Niallia circulans

Inhibitors

Inhibitors Comment Organism Structure
ethanol the enzyme keeps very good levels of alpha-cyclodextrin activity using starch or maltodextrin as substrates even at 20% ethanol (around 55-60%). The degradation of the alpha-cyclodextrin is strongly inhibited by ethanol, even at very low concentrations Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans
-
-
-
Niallia circulans DF 9R
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-cyclodextrin + maltose
-
 Niallia circulans ?
-
 ?
beta-cyclodextrin + maltose
-
 Niallia circulans DF 9R ?
-
 ?
maltodextrin intramolecular transglycosylation Niallia circulans beta-cyclodextrin
-
 ?
maltodextrin intramolecular transglycosylation Niallia circulans DF 9R beta-cyclodextrin
-
 ?
starch intramolecular transglycosylation Niallia circulans beta-cyclodextrin
-
 ?
starch intramolecular transglycosylation Niallia circulans DF 9R beta-cyclodextrin
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 soluble enzyme Niallia circulans
65
-
 enzyme immobilized on glyoxyl-agarose Niallia circulans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
45 70 45°C: soluble enzyme shows about 50% of maximal activity, enzyme immobilized on glyoxyl-agarose shows about 60% of maximal activity, 70°C: soluble enzyme shows about 60% of maximal activity, enzyme immobilized on gyoxyl-agarose shows about 75% of maximal activity Niallia circulans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 if submitted to strong stirring, promoting the apparition of gas bubbles and shear forces, the enzyme becomes inactivated at 25°C. This inactivation does not occur if the enzyme is immobilized on any porous support Niallia circulans
55
-
 half-life of soluble enzyme at pH 7 is 1.5 h. The immobilization of the enzyme on CNBr-agarose does not promote an increment in the stability of the enzyme at 55°C, although it prevents the effect of the stirred system Niallia circulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities Niallia circulans
7
-
 enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities Niallia circulans

pH Range

pH Minimum pH Maximum Comment Organism
4 9 enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities. Activities decrease after these two maximum values. The glyoxyl CGTase retains 30% of amylase activity at pH 4 and 50% at pH 9. The soluble enzyme retains 10% and 30%, respectively. In synthetic activities differences are not significant Niallia circulans