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(1984) as the relative amount of cyclodextrin-trichloroethylene complex that precipitated. The activity of CGTase varied from 22 to 210 dilutions for all strains. The effect of pH on CGTase activity was analyzed over the pH range of 4.5-10.5, under standard conditions (Fig CGTase activity (circle), pH (triangle) and total reducing sugars concentration (square) versus time for enzyme production with immobilized Bacillus firmus strain 37 on bone charcoal. Results: Using the enzyme β-cyclodextrin glycosyltransferase (β-CGTase) as a reporter protein and B. subtilis CCTCC M 2016536 as the host, nine plasmids equipped with single promoters were screened using shake-flask cultivation.

Cgtase activity

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Ca2+ influences the CGTase production and Zn2+ inhibits the enzyme. High CGTase activity was observed at 24 h of.; cyclodextrins; cgtases; starch; synthesis cyclodextrin glucanotransferase, cyclomaltodextrin glucanotransferase, alpha-cgtase, beta- cgtase, toruzyme,  The extracellular enzyme cyclodextrin glucanotransferase (CGTase) synthesizes cyclic Maximum CGTase activity obtained in supernatants was 30.34 U/mL. Growth. We have studied an indigenous bacterial strain produced a glycosyl transfer enzyme.

reported that the γ-CGTase produced by Bacillus clarkii 7364 showed the maximum cyclization activity at pH10.5–11.0, and at 60°C (Takada et al. 2003). Hence, the recombinant γ-CGTase properties, op- The bacterial CGTase was successively purified by acetone precipitation, gel filtration chromatography in a Sephadex G-100 column and ion exchange chromatography in a DEAE-cellulose column.

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Protein concentration was estimated according to Hartree (12), using bovine serum albumin as pattern. 2017-10-10 · The β-CGTase activity in the transformant reached 3885.1UmL-1, which is the highest value reported so far, at 28°C, 6% inoculum ratio, and 1.5% methanol addition following 24h of incubation. The recombinant CGTase showed high specific activity at 80°C without any γ-CGTase activity, and had good stability in a wide pH and temperature range.

Cgtase activity


A 0.1 mL aliquot of appropriately diluted crude enzyme was added to 2 mL of preheated 2% (w/v) soluble starch dissolved in 25 mM phosphate buffer (pH 5.5). CGTase activity produced from Bacillus circulans DF 9R was optimised in shake flasks using a combination of conventional sequential techniques and statistical experimental design. Effects of nutrients, including several carbon, nitrogen and mineral sources, were assayed. The CGTase activity profile was successfully maintained atsteady state using dilution rates of 0.03 to 0.3h-1.

Cgtase activity

In addition, we have revealed the key do-mains responsible for its hydrolytic activity and resistance induction. Further experiments demonstrated that CGTase is a potential func - Polyethylene glycol-6000 showed a 26 % increase in the CGTase activity. The kinetic parameters Km and Vmax were 10 mg/ml and 146 µmol/mg min, respectively, for purified CGTase. CGTase can catalyse four reactions: cyclization, coupling, disproportionation, and hydrolysis (Li et al., 2014b), though the hydrolysis activity is relatively weak (Costa et al., 2009).
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α-CGTase activity was determined using the methyl orange method (Li et al. 2013a, b).

CGTase activity is inhibited by a high substrate concentration and by products formed during reaction,,,,. Therefore, this fact must be taken into account in order to improve the yield and selectivity for CD industrial production. Cyclodextrin glucanotransferases (CGTases; EC have mainly been characterized for their ability to produce cyclodextrins (CDs) from starch in an intramolecular transglycosylation reaction (cyclization).
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For partial purification, the enzyme was  15 Nov 2013 stability compared with free enzyme. The optimum pH for enzyme activity was pH 8 and pH 7.5 for free and immobilized CGTase, respectively,  A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella. This page in English.

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The standard CGTase activity assays described above was used to determine the residual activity of each enzyme (Jeang et al. 2005). Kinetic assays The K m and V max values for the purified enzymes were determined by incubating 100 µL of enzyme (0.5 µg) in 200 µL of 0.2 M phosphate buffer (pH 6.0) with soluble starch solution (0.4–6.0 mg/mL) at 60 °C for 10 min. CGTase activity was assayed as described by Kato and Horikoshi . One unit of enzyme activity was defined as the amount of enzyme that forms 1 μmol of γ-CD from soluble starch in 1 min.