A cyclic activity of accumulation and consumption of beta -CD and gamma -CD occurred during the bacterial growth. CGTase was more active when citrate buffer, pH 5.5 was used. No differences were found for production of gamma -CD with the use of commercial starch flour when compared with corn starch (p>0.05).
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
The double mutant F197Y/G263A showed enhanced coupling activity and displayed a 2-fold increase of the primary coupling product using γ- Interestingly, compared to other CGTases, B. agaradhaerens LS-3C enzyme the hydrolytic activity features of B. agaradhaerens LS-3C CGTase was analyzed. A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella. Zubaida Gulshan Kazi, Pontus keywords: starch: cgtase: cyclodextrin: strain: ncib; Prior art date: 1987-10-15 108040002385 protein O-GlcNAc transferase activity proteins Proteins 0.000 A typical exception from this is the cyclodextrin glucanotransferases(CGTases) which belongs to GH13.This thesis investigates the transglycosylation activity of 1 antibacterial activity of β-cyclodextrin and 2-hydroxypropyl- β-cyclodextrin The cyclization mechanism of cyclodextrin glycosyltransferase (cgtase) as During the last 2 years I focused on protein science, structural biology and protein engineering. Publikationer. A CGTase with high coupling activity using γ- Engineering CGTase to improve synthesis of alkyl glycosides. in a conserved GGHGG loop and allows for comparable α-retaining and β-inverting activity in an Beneficial Activity by Bacillus subtilis. Ramesh C Ray ⋅ Manas R Swain Häftad Production of CGTase from Bacillus subtilis.
An unit of CGTase activity was defined as the amount of enzyme that produces 1 mmol of b-CD per minute, under the assay conditions. The specific activity was expressed in units of activity by milligram of protein. 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 which showed high specific activity at 80°C without any γ-CGTase activity (Zhang et al. 2017).
nitrogen source for CGTase production. Ca2+ influences the CGTase production and Zn2+ inhibits the enzyme.
It was reported that CGTases are active on both starch fractions: amylose and amylopectin but the high amylopectin content were preferred for CGTase activity. (
We discovered that CGTase has antimicrobial activity and induces resistance. 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.
2009-07-08 · Activity characteristics and kinetic aspects of a cyclodextrin glycosyltransferase (CGTase) from Bacillus circulans DF 9R were studied. A mixture of α-, β- and γ-cyclodextrins (CDs), glucose, maltose and negligible amounts of longer linear dextrins were produced from gelatinized amylose, amylopectin and starch from different sources.
Zubaida Gulshan Kazi, Pontus keywords: starch: cgtase: cyclodextrin: strain: ncib; Prior art date: 1987-10-15 108040002385 protein O-GlcNAc transferase activity proteins Proteins 0.000 A typical exception from this is the cyclodextrin glucanotransferases(CGTases) which belongs to GH13.This thesis investigates the transglycosylation activity of 1 antibacterial activity of β-cyclodextrin and 2-hydroxypropyl- β-cyclodextrin The cyclization mechanism of cyclodextrin glycosyltransferase (cgtase) as During the last 2 years I focused on protein science, structural biology and protein engineering. Publikationer. A CGTase with high coupling activity using γ- Engineering CGTase to improve synthesis of alkyl glycosides.
These results strongly support the use of SIFR for CGTase production since it is a non-expensive residue. 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+
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. Alkaline phosphatase was assayed by the method of Yamane et al. [ 9 ].
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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. The plasmid containing the P amyQ' promoter produced the greatest extracellular β-CGTase activity; 24.1 U/mL.
Growth. We have studied an indigenous bacterial strain produced a glycosyl transfer enzyme. (CGTase) yielding polyphenol glycosides from a substrate of
The filtrate containing partially purified CGTase enzyme was analyzed for enzyme activity by the method mentioned below.
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Optimum temperature for maximum CGTase activity was found to be 70 °C as shown in Fig. 6. At temperature higher than 70 °C, activity of CGTase declines sharply may be because the CGTase could be denatured above 70 °C. Relative activity also decreased by about 60% at 80 °C.
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.
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CGTase was expressed by recombinant K. phaffii through pH maintenance in range of 5.5–7.0. β‐CGTase activity increased to 122.0 U/mL after optimization of glycerol, phosphate buffer, pH value, ammonium sulfate, temperature, methanol, and additives based on BSM, establishing a modified defined medium.
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.
CGTase, was selected from B. cereus YUPP-10 by a constructed fos-mid library. We discovered that CGTase has antimicrobial activity and induces resistance. 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 -
process. DNA from the CGTase source organism (E. coli The maximum CGTase activity obtained on SC was 1,155 U mL−1 under aerobic conditions.
CGTase was more active when citrate buffer, pH 5.5 was used. No differences were found for production of gamma -CD with the use of commercial starch flour when compared with corn starch (p>0.05). The enzymes from the α-amylase family all share a similar α-retaining catalytic mechanism but can have different reaction and product specificities.