3.2.1.54: cyclomaltodextrinase
This is an abbreviated version!
For detailed information about cyclomaltodextrinase, go to the full flat file.
Word Map on EC 3.2.1.54
-
3.2.1.54
-
starch
-
cyclodextrins
-
maltose
-
maltodextrins
-
ceramidase
-
neopullulanase
-
transglycosylation
-
thermoactinomyces
-
alpha-amylases
-
maltogenic
-
maltotriose
-
glucanotransferase
-
amylolytic
-
acarbose
-
amylases
-
maltoheptaose
-
malto-oligosaccharides
-
cgtases
-
cyclomaltodextrins
-
maltotetraose
-
panose
-
beta-cd
-
alkalophilic
-
amylomaltase
-
alpha-cd
-
anoxybacillus
-
biotechnology
-
synthesis
-
food industry
-
analysis
- 3.2.1.54
- starch
- cyclodextrins
- maltose
- maltodextrins
- ceramidase
- neopullulanase
-
transglycosylation
-
thermoactinomyces
- alpha-amylases
-
maltogenic
- maltotriose
-
glucanotransferase
-
amylolytic
- acarbose
- amylases
- maltoheptaose
- malto-oligosaccharides
- cgtases
- cyclomaltodextrins
- maltotetraose
- panose
- beta-cd
-
alkalophilic
- amylomaltase
-
alpha-cd
- anoxybacillus
- biotechnology
- synthesis
- food industry
- analysis
Reaction
Synonyms
AfCda13, AglB, alpha-amylase, alpha-amylase II, CD-/pullulan-hydrolyzing enzyme, CD-ase, CD-degrading enzyme, CD-hydrolyzing amylase, CDA, CDase, CDase I-5, CMD, cyclodextrinase, cycloheptaglucanase, cyclohexaglucanase, cyclomaltodextrin dextrin-hydrolase, Cyclomaltodextrin hydrolase, decycling, cyclomaltodextrinase, CymH, cytoplasmic decycling maltodextrinase, EC 3.2.1.12, Env cda13A, FspCMD, H-17 CDase, H-17 thermostable CDase, LLCD, LsCda13, Lsp26X-Mdase, maltodextrin glucosidase, More, neopullulanase, PFTA, RA.04, thermophilic CDase, TK1770, TVA II
ECTree
Advanced search results
General Stability
General Stability on EC 3.2.1.54 - cyclomaltodextrinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
denaturation and unfolding induced with 2 M guanidine hydrochloride pH 7.0 or 25 mM glycine phosphate buffer, pH 2 for 4 h at 25°C, chaperons GroEL, GroES assist in vivo and in vitro folding of the enzyme, a trans folding mechanism for GroEL/GroES-assisted refolding of MalZ is proposed
-
more than 90% of the enzyme activity remains in the pH range of 8.0-10.0 and at 4°C in the absence of CaCl2 after pH and temperature treatments, respectively. Cda is efficiently stabilized by CaCl2. In the presence of CaCl2. Cda is stable in the pH range of 7.0-10.5 and at temperatures below 30°C.
pH 7.0, 8 M urea and 20 mM dithiothreitol, glycerol, dimethylsulfoxide, trimethylamine-N-oxide, trehalose and proline act as chemical chaperones in the refolding of the denatured MalZ, GroEL, GroES and ATP-mediated refolding of urea
-
stable in the presence of up to 2% Triton X-100, completely inactivated in the presence of SDS at concentrations higher than 50 mM
additional information
-