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Cyclodextrin glucanotransferase (CGTase) activity was observed when the bacterium was grown in the medium at various initial pH values, containing carbon, nitrogen, phosphorus and mineral salt sources at 50 oC for 24 h in the shake flasks. The optimisation of this growth medium was carried out using response surface methodology.

The CGTase activity was increased in the presence of metal ions (5 mM): Ca+2 (130 %), Mg+2 (123 %), Mn+2 (119 %) and Co+2 (116 %). The enzyme activity was strongly inhibited in the presence of Hg+ The β-CGTase from alkalophilic Bacillus sp. N-227 was separately mutagenized to give three site-directed β-CGTase mutants, Y127F, R254F and D355R, that showed enhanced cyclization activity towards a starch substrate from 1.64 to 2.1-folds. Kinetic studies indicate that the mutants had higher affinity towards the substrate than the wild type The optimum temperature of CGTase activity increased from 50 to 60 °C after the stabilizer application. The stabilizer was applied to cyclodextrin production, and it resulted in enhanced CGTase activity, which showed higher increases of starch to CD conversion at 60 and 90 °C.

Thus, the activity half-life of this enzyme can be enhanced by The enzyme variant is obtainable by modifying a CGTase or a maltogenic glycosyltransferase (CGTase) polypeptides with modified hydrolysis activity 8 Jun 2017 β-CGTase is one of the important α-amylase family, and CGTase is the first enzyme of all the transglycosylases. In general, the cyclization activity The CGTase activity was measured as β-cyclodextrin. (β-CD) forming activity by the PHP method [33]. Fifty- microliters crude enzyme were added to 1 ml of 2%. yeast extract, peptone and starch showed highest impact on the CGTase production.

CGTase activity.

C-niveau - KVUC Bild. EP2316929B1 - Maltogenic alpha-amylase variants - Google Patents. Effect of storage temperature on -amylase activity from .

inactivated by heat and is removed completely during the a-CD production . process. DNA from the CGTase source organism (E.

A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella. Zubaida Gulshan Kazi, Pontus

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 2.4.1.19) have mainly been characterized for their ability to produce cyclodextrins (CDs) from starch in an intramolecular transglycosylation reaction (cyclization). γ-Cyclodextrin glycosyltransferase (γ-CGTase) catalyzes the biotransformation of low-cost starch into valuable γ-cyclodextrin (γ-CD), which is widely applied in biotechnology, food, and pharmaceutical industries. CGTase activity was assayed as described by Kato and Horikoshi [ 5 ]. 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.

α-CGTase activity assay. α-CGTase activity was determined using the methyl orange method (Li et al. 2013a, b). The culture supernatant (0.1 mL) was mixed with 0.9 mL of 5% (w/v) soluble starch in 50 mM phosphate buffer (pH 6.0) and incubated at 40 °C for 10 min. D-xylose.
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Fifty- microliters crude enzyme were added to 1 ml of 2%.
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A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella. Gulshan Kazi, Zubaida LU; Lundemo, Pontus LU; Fridjonsson, Olafur H; Hreggvidson, Gudmundur O; Adlercreutz, Patrick LU and Nordberg Karlsson, Eva LU () In Glycobiology 25 (5). p.514-523

We have determined the 2.0 and 2.5 Angstrom X-ray structures of E257A/D229A CGTase in complex with maltoheptaose and maltohexaose. At this point the total soluble γ-CGTase activity had reached 5.51 U·mL − 1. In addition, the ratio of extracellular γ-CGTase activity to total γ-CGTase activity decreased from 71.7 to 55.0% when the concentration of β-cyclodextrin increased from 0 to 10 mM. lower the CGTase activity.

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nitrogen source for CGTase production. Ca2+ influences the CGTase production and Zn2+ inhibits the enzyme. High CGTase activity was observed at 24 h of.

The precipitate was collected by centrifugation (27,000 × g for 30 min), dissolved in 25 mM Tris-HCl buffer (pH 7.0) containing 12% ammonium sulfate saturation, and applied to a phenyl-Superose HR 5/5 column (Pharmacia) previously equilibrated with the same buffer. Estimation of CGTase Activity CGTase activity was measured using phenolphthalein β-cyclodextrin complexation method20.

The CGTase production was further studied with the optimized process parameters on submerged cultivations (SC) and solid-state cultivations (SSC) using soybean industrial fibrous residue (SIFR). The maximum CGTase activity obtained on SC was 1,155 U mL−1 under aerobic conditions. Cell growth and CGTase synthesis in SSC using SIFR as substrate After three rounds of mutagenesis the hydrolytic activity had increased 90-fold, reaching the highest hydrolytic activity ever reported for a CGTase. The single mutation with the largest effect (A230V) occurred in a residue not studied before. 2017-02-20 · α-CGTase activity.