Results 121 to 130 of about 593 (163)
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Applied Biochemistry and Biotechnology, 2007
Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) was immobilized using different supports and immobilization methods to study the effect on activity recovery. The enzyme covalently attached into glyoxyl-silica showed low activity recovery of 1.5%.
Ana Elisa, Amud +5 more
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Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) was immobilized using different supports and immobilization methods to study the effect on activity recovery. The enzyme covalently attached into glyoxyl-silica showed low activity recovery of 1.5%.
Ana Elisa, Amud +5 more
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Immobilized cyclomaltodextrin glucanotransferase of an alkalophilic Bacillus sp. No. 38‐2
Biotechnology and Bioengineering, 1984AbstractCyclomaltodextrin glucanotransferase [1,4‐α‐D‐glucan‐4‐α‐D‐(1,4‐α‐D‐glucano)–transferase (cyclizing), E.C.−2.4.1.19] of an alkalophilic Bacillus sp. No. 38‐2 (ATCC 21783), which contains three types of enzymes (acid, neutral, and alkaline enzymes), was immobilized on synthetic adsorption resin.
T, Kato, K, Horikoshi
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Journal of Biochemical and Biophysical Methods, 1990
The catalytically active subforms of cyclomaltodextrin glucanotransferase (CGTase; EC 2.4.1.19) from Bacillus circulans var. alkalophilus and from a strain in which the CGTase expressing gene had been cloned were studied by using isoelectric focusing (IEF) in immobilized and in conventional pH gradients. Even with high protein loads the best resolution
P, Mattsson, S, Meklin, T, Korpela
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The catalytically active subforms of cyclomaltodextrin glucanotransferase (CGTase; EC 2.4.1.19) from Bacillus circulans var. alkalophilus and from a strain in which the CGTase expressing gene had been cloned were studied by using isoelectric focusing (IEF) in immobilized and in conventional pH gradients. Even with high protein loads the best resolution
P, Mattsson, S, Meklin, T, Korpela
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Applied Biochemistry and Biotechnology, 2007
A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and moderately thermophilic Paenibacillus campinasensis strain H69-3 was purified as a homogeneous protein from culture supernatant. Cyclomaltodextrin glucanotransferase was produced during submerged fermentation at 45 degrees C and purified by gel filtration on ...
Alves-Prado, Heloiza Ferreira +2 more
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A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and moderately thermophilic Paenibacillus campinasensis strain H69-3 was purified as a homogeneous protein from culture supernatant. Cyclomaltodextrin glucanotransferase was produced during submerged fermentation at 45 degrees C and purified by gel filtration on ...
Alves-Prado, Heloiza Ferreira +2 more
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The Formation of Amylose-Granules from Cyclomaltodextrin Glucanotransferase by .ALPHA.-Cyclodextrin.
Journal of the Japanese Society of Starch Science, 1993B. stearothermophzlus由来のCGTaseを高濃度のα-CDに作用させることによりアミロース粒子が生成することを見出し,その生成条件ならびにその諸性質を調べ,以下の結果を得た.1) アミロース粒子の生成は,主に反応温度,基質濃度に影響され,α-CD濃度35%,反応温度30℃で最高の生成率96%を示した.2) 他の細菌起源のCGTaseにおいてもアミロース粒子の生成が認められた.3) 得られるアミロース粒子は3～20gumの球状で,そのλmaxは560～580nmを示し,数平均分子量は5500～7000で,グルコース・ユニットとして34～43個からなるアミロースであった.4) 本物質はX線回折により澱粉のB形X線回折図を示し ...
Takashi SHIBUYA +5 more
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[New cyclomaltodextrin-glucanotransferases, produced by Bacillus macerans].
Prikladnaia biokhimiia i mikrobiologiia, 2000For the first time, microorganisms producing cyclomaltodextrin glucan transferases (CGT, EC 2.4.1.19) were isolated from soil samples of various ecogeographical regions. These microorganisms were identified as Bacillus macerans. The enzymes were purified by affinity chromatography on a alpha-cyclodextrin polymer and gel filtration on Biogel P-450 and ...
V A, Abelian, K B, Afian, L S, Manukian
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Applied Microbiology and Biotechnology, 1992
The cyclomaltodextrin glucanotransferase (CGTase, E.C. 2.4.1.19) gene from an alkalophilic Bacillus circulans var. alkalophilus ATCC21783 was cloned into Escherichia coli and B. subtilis. When cloned from E. coli to B. subtilis, the entire insert containing the CGTase gene was, depending on the plasmid construction, either unstable or the recombinant B.
M, Paloheimo +3 more
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The cyclomaltodextrin glucanotransferase (CGTase, E.C. 2.4.1.19) gene from an alkalophilic Bacillus circulans var. alkalophilus ATCC21783 was cloned into Escherichia coli and B. subtilis. When cloned from E. coli to B. subtilis, the entire insert containing the CGTase gene was, depending on the plasmid construction, either unstable or the recombinant B.
M, Paloheimo +3 more
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A novel cyclomaltodextrin glucanotransferase from Bacillus firmus that degrades raw starch
Biotechnology Letters, 1995An alkalophilic Bacillus firmus secreting the enzyme cyclomaltodextrin glucanotransferase was isolated from soil. The enzyme attacked raw starch to produce cyclodextrins. Maximum cyclodextrins were produced from tapioca starch followed by potato and corn starch. About 49 % of tapioca starch (at 10 and 50 g/l) was converted to cyclodextrins.
Anuj Goel, Sanjay Nene
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Purification and properties of beta‐cyclomaltodextrin glucanotransferase from Bacillus flexus SV 1
Journal of Basic Microbiology, 2017Cyclomaltodextrin glucanotransferase is a unique enzyme that degrades starch into cyclic oligosaccharides called cyclodextrins, which have numerous applications in various industries such as pharmaceutical, textile, agricultural, cosmetics etc.
Shwetha V. Reddy +2 more
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Wei sheng wu xue bao = Acta microbiologica Sinica, 2003
A cyclomaltodextrin glucanotransferase from alkaliphilic bacteria was purified to PAGE homogenous by ammonium sulfate precipitation and DEAE-cellulose DE-52 chromatography with 11.5 fold purification and 5.7% recovery. Mr estimated with concentration gradient PAGE was 151,000.
Q, Zhang, Z, Yan, S, Zhang
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A cyclomaltodextrin glucanotransferase from alkaliphilic bacteria was purified to PAGE homogenous by ammonium sulfate precipitation and DEAE-cellulose DE-52 chromatography with 11.5 fold purification and 5.7% recovery. Mr estimated with concentration gradient PAGE was 151,000.
Q, Zhang, Z, Yan, S, Zhang
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