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
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3.2.1.54
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starch
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cyclodextrins
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maltose
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maltodextrins
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ceramidase
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neopullulanase
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transglycosylation
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thermoactinomyces
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alpha-amylases
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maltogenic
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maltotriose
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glucanotransferase
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amylolytic
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acarbose
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amylases
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maltoheptaose
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malto-oligosaccharides
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cgtases
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cyclomaltodextrins
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maltotetraose
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panose
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beta-cd
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alkalophilic
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amylomaltase
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alpha-cd
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anoxybacillus
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biotechnology
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synthesis
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food industry
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analysis
- 3.2.1.54
- starch
- cyclodextrins
- maltose
- maltodextrins
- ceramidase
- neopullulanase
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transglycosylation
-
thermoactinomyces
- alpha-amylases
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maltogenic
- maltotriose
-
glucanotransferase
-
amylolytic
- acarbose
- amylases
- maltoheptaose
- malto-oligosaccharides
- cgtases
- cyclomaltodextrins
- maltotetraose
- panose
- beta-cd
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alkalophilic
- amylomaltase
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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
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Application
Application on EC 3.2.1.54 - cyclomaltodextrinase
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analysis
biotechnology
food industry
synthesis
additional information
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synthesis of radiolabeled linear and cyclic maltodextrins as tools for metabolism investigation
analysis
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synthesis of radiolabeled linear and cyclic maltodextrins as tools for metabolism investigation
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Archaeoglobus fulgidus utilizes an unusual pathway of starch degradation involving cyclodextrins as intermediates, extracellular cyclodextrins are transported into the cell and linearized via a CDase
biotechnology
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chemical or molecular operones can be used in refolding of various aggregate-prone proteins of commercial and medical importance after overexpression in Escherichia coli
biotechnology
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Archaeoglobus fulgidus utilizes an unusual pathway of starch degradation involving cyclodextrins as intermediates, extracellular cyclodextrins are transported into the cell and linearized via a CDase
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the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry
food industry
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the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry
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CDase I-5 is applied to modify the starch structure to produce low-amylose starch products by incubating rice starch with this enzyme. The amylose content of rice starch decreases from 28.5 to 9% while the amylopectin content remains almost constant with no significant change in side chain length distribution
synthesis
the G415E mutant is an excellent candidate for the industrial production of specific-length maltooligosaccharides from cyclodextrins
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neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
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neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates