Results 111 to 120 of about 593 (163)
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Maltodextrin-dependent crystallization of cyclomaltodextrin glucanotransferase from Bacillus circulans

Journal of Molecular Biology, 1990
Crystals of cyclomaltodextrin glucanotransferase from Bacillus circulans (EC 2.4.1.19) suitable for high-resolution X-ray analysis were obtained by vapor diffusion against 60% (v/v) 2-methyl 2,4-pentanediol buffered with 100 mM-sodium Hepes, pH 7.55. The crystals have P2(1)2(1)2(1) space group symmetry, with a = 120.4 A, b = 110.9 A and c = 66.4 A, and
Lawson, Catherine L.   +5 more
openaire   +2 more sources

Cyclomaltodextrin Glucanotransferase-Catalyzed Transglycosylation from Dextrin to Alkanol Maltosides

Bioscience, Biotechnology, and Biochemistry, 2008
Maltosides of butanol, octanol, and lauryl alcohol were found for the first time to serve as substrates for cyclomaltodextrin glucanotransferase (CGTase), and glycosyl residue was transfered from dextrin to the substrate affording novel maltosides with 3-4 glucose units.
Haisuo, Zhao   +7 more
openaire   +2 more sources

Cyclomaltodextrin glucanotransferase-producing moderate thermophile, Bacillus coagulans

Journal of Fermentation and Bioengineering, 1991
Abstract A new CGTase-producing moderate thermophile was isolated from soil, and was identified as Bacillus coagulans which have not previously been listed as cyclodextrin producing bacteria. The culture filtrate of the isolate as the CGTase source converted about 60% of soluble starch to CD's in 20 h at 50°C, and the ratio of α-: β-: γ-CD produced
Kunihiro Akimaru   +2 more
openaire   +1 more source

Optimization of cyclomaltodextrin glucanotransferase production from Bacillus firmus

Enzyme and Microbial Technology, 1998
Abstract Production of cyclomaltodextrin glucanotransferase (CGTase) from Bacilus firmus was optimized in shake flasks using a statistical experimental design approach. Two level complete factorial designs in three variables were used for media optimization.
B.N. Gawande   +4 more
openaire   +1 more source

Chemical modification of cyclomaltodextrin glucanotransferase from Bacillus circulans var. alkalophilus

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
Counting of integral numbers of cysteine residues of the reduced and denaturated form of cyclomaltodextrin glucanotransferase (CGTase) from Bacillus circulans var. alkalophilus (ATCC 21783) showed two cysteine residues per enzyme molecule. Titrations of the enzyme with 5,5'-dithiobis-(2-nitrobenzoic acid) led to the same result.
P, Mattsson, T, Pohjalainen, T, Korpela
openaire   +2 more sources

Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192: nitration with tetranitromethane

Biotechnology and Applied Biochemistry, 1993
Nitration of tyrosine residues was performed on Bacillus circulans E 192 cyclomaltodextrin glucanotransferase (CGTase) using tetranitromethane (TNM). A maximum of 15 out of 28 tyrosine residues is modified with 8 mM TNM, entailing a concomitant loss of enzymic activity and tryptophan fluorescence.
J R, Villette   +4 more
openaire   +2 more sources

Synthesis of Glycosyl-trehaloses by Cyclomaltodextrin Glucanotransferase through the Transglycosylation Reaction

Bioscience, Biotechnology, and Biochemistry, 1997
Cyclomaltodextrin glucanotransferase from Bacillus stearothermophilus produced a series of glycosyl-trehaloses through the transglycosylation reaction with cyclomaltohexaose as the glycosyl donor and trehalose as its acceptor. After beta-amylase treatment, five species of glycosyl-trehaloses were isolated by column chromatography.
M, Kurimoto   +7 more
openaire   +2 more sources

Purification and properties of Bacillus coagulans cyclomaltodextrin glucanotransferase

Journal of Fermentation and Bioengineering, 1991
Abstract Cyclomaltodextrin glucanotransferase (CGTase), produced in a culture filtrate by Bacillus coagulans , was purified to a single, homogeneous protein. It has a monomeric structure with a molecular weight of 65,000, isoelectric point of 4.6, and contains 2 mol of Ca 2+ per mol of the enzyme.
Kunihiro Akimaru   +2 more
openaire   +1 more source

Characterization of Thermoanaerobacter cyclomaltodextrin glucanotransferase immobilized on glyoxyl-agarose

Enzyme and Microbial Technology, 2006
Abstract This paper presents the immobilization of the Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) enzyme into cross-linked 6% agarose beads activated by high density of linear aldehyde groups (glyoxyl-agarose) that allow the establishment of multi-attachment enzyme-support bonds.
Paulo W. Tardioli   +2 more
openaire   +1 more source

Determination of the catalytic activity of cyclomaltodextrin glucanotransferase by maltotriose-methylorange assay

Journal of Biochemical and Biophysical Methods, 1988
A kinetic assay of cyclomaltodextrin glucanotransferase (EC 2.4.1.19), based on the use of methylorange dye as the indicator of cyclodextrins, was studied and the reaction verified with independent HPLC analyses. The assay was optimized for the enzyme of an alkalophilic Bacillus sp. (ATCC 21783).
M J, Mäkelä, T K, Korpela
openaire   +2 more sources

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