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2.4.1.19: cyclomaltodextrin glucanotransferase

This is an abbreviated version!
For detailed information about cyclomaltodextrin glucanotransferase, go to the full flat file.

Word Map on EC 2.4.1.19

Reaction

alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose
=
alpha-cyclodextrin
+
alpha-D-glucose

Synonyms

1,4-alpha-D-glucopyranosyl transferase, Akrilex C cyclodextrin glycosyltransferase, alpha-1,4-glucan 4-glycosyltransferase, cyclizing, alpha-cgt, alpha-CGTase, alpha-cyclodextrin glucanotransferase, alpha-cyclodextrin glucosyltransferase, alpha-cyclodextrin glycosyltransferase, Bacillus macerans amylase, beta-CGTase, beta-cyclodextrin glucanotransferase, beta-cyclodextrin glucosyltransferase, beta-cyclodextrin glycosyltransferase, beta-cyclodextrinase, BMA, C-CGTase, CD glucanotransferase, CGT, CGT13, CGTase, cgtS, CGTse ET1, CGT_TK, cyclodextrin beta-glucanotransferase, cyclodextrin glucanotransferase, cyclodextrin glucosyltransferase, cyclodextrin glycosyl transferase, cyclodextrin glycosyltransferase, cyclodextrin-glycosyltransferase, cyclodextrinase, cyclomaltodextrin glucanyltransferase, cyclomaltodextrin glucotransferase, cyclomaltodextrin glycanotransferase, cyclomaltodextrin glycosyltransferase, gamma-CGTase, gamma-cyclodextrin glycosyltransferase, konchizaimu, M-CGTase, More, neutral-cyclodextrin glycosyltransferase, PFCGT, Toruzyme

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.19 cyclomaltodextrin glucanotransferase

General Stability

General Stability on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATCC 2178, exceptionally stable
-
Ca2+ stabilizes against thermal inactivation, 5 mM CaCl2 shifts the apparent melting point from 60°C to 69°C
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Ca2+, 20 mM, increases thermal stability
-
cell membrane-immobilized purified enzyme retains, after 240 h repeated batch cultivation, 1.3-2.3fold increase of the CGTase yield compared to free cells at the end of the process, overview
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cross-linked enzyme crystals are slightly more resistant to 2-butanol and acetonitrile than DMSO. In 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 28% of the activity remains in the case of soluble CGTase
-
enzyme immobilized on alginate shows a high operational stability by retaining almost 75% of the initial activity after seventh use
-
enzyme stability is greatly enhanced with sorbitol
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high substrate concentrations stabilize against thermal inactivation
-
immobilization in strongly hydrophilic microenvironment markedly enhances conformational stability in a wide temperature and pH range
-
more than 80% of the initial immobilized and crosslinked imprinted CGTase activity is retained for up to five cycles of synthesis reactions
not inactivated by 2 M guanidium chloride
-
prolonged digestion with trypsin does not affect the catalytic properties
-
relatively stable to Hg2+
-
SDS, 1%, only 7% of the activity of soluble enzyme activity remains, cross-linked enzyme crystals exhibit strong activity
-
the dextran (MW 47000)-conjugated form of the enzyme retains about 70.28% of the original specific catalytic activity exhibited by the native enzyme
-
the immobilized and CD8-crosslinked imprinted CGTase shows 15% higher stability in phosphate buffer containing up to 50% ethanol or cyclohexane compared to the native enzyme
-
the immobilized and CD8-crosslinked imprinted CGTase shows 30% higher stability in phosphate buffer containing up to 50% ethanol or cyclohexane compared to the native enzyme
-
the operational half-life of the packed-bed enzyme reactor (enzyme immobilized onto a cation exchanger by ionic interaction, poly-lysine fused immobilization) is estimated 12 days at 25°C and pH 6.0
-
the temperature stability of the immobilized and crosslinked imprinted CGTase at 60°C is considerably higher than that of the native enzyme
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
-