Results 41 to 50 of about 2,428 (190)
Comparison of CD composition produced by chimeric CGTases.
Agricultural and Biological Chemistry, 1990 Using 12 chimeric cyclomaltodextrin glucanotransferases (CGTases) constructed from two genes, the CGTase gene from the alkalophilic Bacillus sp. strain No. 38-2 (CGTase 38-2 gene) and the CGTase gene from the alkalophilic Bacillus sp. strain No. 17-1 (CGTase 17-1 gene), we compared the effect of those chimeric enzymes on cyclodextrin (CD) production ...
T, Kaneko, T, Kudo, K, Horikoshi
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Microbial Cell Factories, 2017 Background Cyclodextrin glucanotransferases (CGTases) catalyze the synthesis of cyclodextrins, cyclic oligosaccharides composed of glucose monomers that find applications in the pharmaceutical, food, and cosmetic industries.
Christian Sonnendecker +5 more
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Optimization of medium for the production of β-cyclodextrin glucanotransferase using Central Composite Design (CCD) [PDF]
, 2005 Production of cyclodextrin glucanotransferase (CGTase) from Bacillus G 1, a new bacterial isolate was optimized in shake-flask cultures using statistical design approach. An efficient fermentation medium producing CGTase with high activity (54.9U/ml) was
Abdul Hamid, Aidil +5 more
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Conversion of the maltogenic α-amylase Novamyl into a CGTase [PDF]
Protein Engineering, Design and Selection, 2000 Novamyl is a thermostable five-domain maltogenic alpha-amylase that shows sequence and structural homology with the cyclodextrin glycosyltransferases (CGTases). Comparing X-ray crystal structures of Novamyl and CGTases, two major differences in the active site cleft were observed: Novamyl contains a loop insertion consisting of five residues (residues ...
L, Beier +5 more
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Physico-chemical properties of corn starch modified with cyclodextrin glycosyltransferase [PDF]
, 2016 Cyclodextrin glycosyltransferase (CGTase) has been used to produce cyclodextrins (CDs) from starches, but their ability to modify starches has been barely explored.
Durá, Ángela, Rosell, Cristina M.
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Cyclization Reaction of CGTase on Amylose.
Journal of Applied Glycoscience, 1999 The Cyclization reaction of cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) from alkalophilic Bacillus sp. A2-5a, Bacillus macerans, and Bacillus stearothermophilus on amylose was reinvestigated by the use of high-performance anion exchange chromatography . When CGTase from alkalophilic Bacillus sp.
Yoshinobu Terada +5 more
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Processo para produção de ciclodextrinas por CGTase semipurificada [PDF]
Anais do V Simpósio de Bioquímica e Biotecnologia, 2015 Introducao: A ciclodextrina glicosiltransferase (CGTase) e uma importante enzima de interesse industrial, unica em sua capacidade de converter o amido em ciclodextrinas (CDs). As CDs sao malto-oligossacarideos ciclicos capazes de formar complexos de inclusao com um grande numero de substâncias, o que as torna atraentes para varias aplicacoes ...
Vanderson Carvalho Fenelon +5 more
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Journal of the Japanese Society of Starch Science, 1986 Three kinds of cyclomaltodextrin glucanotransferases (CGTases) produced by Bacillus ohbensis, Bacillus macerans and Bacillus circulans were respectively purified to a single protein and the CGTase from B. ohbensis was successfully crystallized. Comparative studies of three CGTases revealed that the CGTase from B.
Yoshiaki YAGI +2 more
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Combination of extrusion and cyclodextrin glucanotransferase treatment to modify wheat flours functionality [PDF]
, 2016 This research aims to vary functional properties of native and extruded wheat flours combining cyclodextrin glucanotransferase and extrusion treatments.
Durá, Ángela +4 more
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Thermoanaerobacter sp. CGTase: Its Properties and Application.
Journal of the Japanese Society of Starch Science, 1992 A novel CGTase (Cyclomaltodextrin glucanotransferase) has been isolated from a strain of Thermoanaerobacter, a thermophilic anaerobe. The enzyme is extremely heat stable and has a temperature optimum of 90-95°C at pH 6.0. It is active over a broad pH range, and exhibits more than 80% activity from pH 5.0-6.7.
Barrie E.NORMAN, Steen T.JØRGENSEN
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