Results 131 to 140 of about 593 (163)
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Analytical Biochemistry, 1986
A mixture of p-nitrophenyl O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranoside (FG5P) and p-nitrophenyl alpha-D-glucoside (GP) was incubated with cyclomaltodextrin glucanotransferase (CGTase) [EC 2.4.1.19 ...
S, Satomura, K, Omichi, T, Ikenaka
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A mixture of p-nitrophenyl O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranoside (FG5P) and p-nitrophenyl alpha-D-glucoside (GP) was incubated with cyclomaltodextrin glucanotransferase (CGTase) [EC 2.4.1.19 ...
S, Satomura, K, Omichi, T, Ikenaka
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Biotechnology and Applied Biochemistry, 1992
The cyclomaltrodextrin glucanotransferase (CGTase) [1,4‐alpha‐D‐glucan:4‐alpha‐D‐(1,4‐alpha‐D‐glucano)‐transferase (cyclizing), EC 2.4.1.19] from Bacillus circulans E 192 has been purified to homogeneity by Cetavlon treatment, ammonium sulfate precipitation, DEAE Trisacryl M chromatography, Q Fast Flow chromatography, and affinity on beta‐cyclodextrin ...
L J, Bovetto +4 more
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The cyclomaltrodextrin glucanotransferase (CGTase) [1,4‐alpha‐D‐glucan:4‐alpha‐D‐(1,4‐alpha‐D‐glucano)‐transferase (cyclizing), EC 2.4.1.19] from Bacillus circulans E 192 has been purified to homogeneity by Cetavlon treatment, ammonium sulfate precipitation, DEAE Trisacryl M chromatography, Q Fast Flow chromatography, and affinity on beta‐cyclodextrin ...
L J, Bovetto +4 more
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Applied Microbiology and Biotechnology, 1999
A novel raw starch degrading cyclomaltodextrin glucanotransferase (CGTase; E.C. 2.4.1.19), produced by Bacillus firmus, was purified to homogeneity by ultrafiltration, affinity and gel filtration chromatography. The molecular weight of the pure protein was estimated to be 78,000 and 82,000 Da, by SDS-PAGE and gel filtration, respectively.
B N, Gawande +3 more
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A novel raw starch degrading cyclomaltodextrin glucanotransferase (CGTase; E.C. 2.4.1.19), produced by Bacillus firmus, was purified to homogeneity by ultrafiltration, affinity and gel filtration chromatography. The molecular weight of the pure protein was estimated to be 78,000 and 82,000 Da, by SDS-PAGE and gel filtration, respectively.
B N, Gawande +3 more
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Journal of Biotechnology, 1992
A plasmid expression vector was constructed to direct the synthesis of foreign proteins in Escherichia coli as fusions with cyclomaltodextrin glucanotransferase (CGT) with cytoplasmic location (delta ssCGT). The ability of CGT to bind to covalently immobilized cyclodextrins was utilized in purifying fused target proteins.
J, Hellman +2 more
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A plasmid expression vector was constructed to direct the synthesis of foreign proteins in Escherichia coli as fusions with cyclomaltodextrin glucanotransferase (CGT) with cytoplasmic location (delta ssCGT). The ability of CGT to bind to covalently immobilized cyclodextrins was utilized in purifying fused target proteins.
J, Hellman +2 more
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Carbohydrate Research, 2002
It was found that Bacillus macerans cyclomaltodextrin glucanotransferase (CGTase) reacts with cyclomaltohexaose (alpha-cyclodextrin, alpha-CD) to give a series of cyclomaltooligosaccharides (cyclomaltodextrins, CDs), having seven to more than 20 D-glucose residues and maltooligosaccharides (maltodextrins, MDs) from G5 to G12+.
Seung-Heon, Yoon, John F, Robyt
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It was found that Bacillus macerans cyclomaltodextrin glucanotransferase (CGTase) reacts with cyclomaltohexaose (alpha-cyclodextrin, alpha-CD) to give a series of cyclomaltooligosaccharides (cyclomaltodextrins, CDs), having seven to more than 20 D-glucose residues and maltooligosaccharides (maltodextrins, MDs) from G5 to G12+.
Seung-Heon, Yoon, John F, Robyt
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Canadian Journal of Microbiology, 1990
The time course of the growth of cyclomaltodextrin glucanotransferase (EC 2.4.1.19; CGTase) producing Bacillus circulans var. alkalophilus (ATCC 21783) was studied using shaking-flask cultivations. The growth curve was diauxic and during the initial phase the pH decreased sharply by 1.3–1.5 units.
Mauri J. Mäkelä +2 more
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The time course of the growth of cyclomaltodextrin glucanotransferase (EC 2.4.1.19; CGTase) producing Bacillus circulans var. alkalophilus (ATCC 21783) was studied using shaking-flask cultivations. The growth curve was diauxic and during the initial phase the pH decreased sharply by 1.3–1.5 units.
Mauri J. Mäkelä +2 more
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Cyclomaltodextrin glucanotransferase variants
The present invention relates to variants of cyclomaltodextrin glucanotransferase. More specifically, the invention relates to a maethod of modifying the substrate binding and/or product selectivity of a precursor CGTase enzyme, and CGTase variants derived from a precursor CGTase enzyme by substitution, insertion and/or deletion of one or more amino ...Dijkhuizen, Lubbert +3 more
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Integrative oncology: Addressing the global challenges of cancer prevention and treatment
Ca-A Cancer Journal for Clinicians, 2022Jun J Mao,, Msce +2 more
exaly
Some properties of a cyclomaltodextrin-glucanotransferase from Bacillus circulans DF 9 R type.
Cellular and molecular biology (Noisy-le-Grand, France), 1997The cyclomaltodextrin-glucanotransferase (EC2.4.1.19, CGTase) which was purified to homogeneity from Bacillus circulans strain DF 9, R type, showed a pI of 5.3 determined by disc-isoelectric focusing, a Mw of 78 kDa estimated by SDS-PAGE with a range of pH of optimal enzymatic activity rather large (4.5-7.5).
L R, Maréchal +4 more
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