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Wang et al. added β-CD as a chemical chaperone to the cul-ture medium and observed the yield of soluble γ-CGTase cyclization activity to be 50.29U mL−1(Wang et al. 2018a). CGTase production can be improved by manipulating fermentation conditions such as pH, temperature, concentrations of nutrients and compositions of the production media (carbon and nitrogen sources). Sivakumar and Shakilabanu (2013) found that maltose was the best carbon source and yeast extract was the best nitrogen source for CGTase production using B. megaterium . CGTase Production The CGTase production pattern by isolated Bacillus sp.

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In order to verify the effect of sodium ion on the CGTase production strains were grown in the same medium replacing Na 2CO 3 by NaCl, at pH 7.0. Qualitative analysis of CGTase The CGTase production process consists of a submerged culture fermentation using the recombinant producer organism Bacillus licheniformis strain SJ1608, the stock culture and fermentation culture both being controlled frequently for identity of the organism, absence of contaminating microorganisms, and enzyme yield before harvesting the enzyme. The Bacillus macerans cyclodextrin glycosyltransferase (CGTase) (EC 2.4.1.19) was covalently immobilised on Eupergit C and used in a packed-bed reactor to investigate the continuous production of long-carbohydrate-chain alkyl glycosides from alpha-cyclodextrin (alpha-CD) and n-dodecyl-(1,4)-beta-maltopyranoside (C(12)G(2)beta). The US132 CGTase production monitored after 18 hours of induction showed that the use of M9ZB and 2TY medium increased the production by about 1.1-fold (16.5 U/mL) and 1.3-fold (20 U/mL), respectively, in comparison to that obtained by LB broth. However, the use of M9 medium decreased the production to attain only 8 U/mL. CGTase overexpression enabled a burst of reactive oxygen species production and activated pathogenesis-related gene expression, indicating that the transgenic cotton was better prepared to protect itself from infection. CGTase production was the same with either organic nitrogen or inorganic nitrogen source.

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Production of Cgtase from Bacillus Subti: Kumaraswamy, Bhargav

Extracellular production of CGTase is usually achieved by expression in the native Bacillus host or by targeting the protein to the periplasmic space followed by release to the extracellular medium through the weakening of E. coli cell envelope. 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.

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Cyclodextrin glucanotransferase (CGTase, EC 2.4.1.9) is an unique enzyme capable of converting starch and related substrates into cyclodextrins (CDs). In this paper, we report an one step gel purification method of CGTase from Bacillus sp. and later enzyme characterization. The Bacillus sp. strain was isolated from a Colocacia esculenta rizospheric soil sample and the CGTase production was In view of this, effect of tapioca starch on CGTase production by the alkalophile was evaluated.

The Bacillus sp. strain was isolated from a Colocacia esculenta rizospheric soil sample and the CGTase production was In view of this, effect of tapioca starch on CGTase production by the alkalophile was evaluated. From our findings, low concentration of tapioca starch (1% w/v) gives higher CGTase production. Illias et al 24 reported maximum CGTase production with 1% tapioca starch as the carbon source for Bacillus sp.
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TS1-1 was grown in a medium containing sago starch, yeast extract, phosphorus and mineral salt sources, using shake flask mode at 37 °C for 24 h. Cyclodextrin glycosyltransferase (CGTase; E.C. 2.4.1.19) is an industrially important enzyme, which is used to produce cyclodextrins (CDs). In this research, we report the use of experimental factorial design to find the best conditions of pH and temperature for CGTase production by Bacillus circula … The γ-CGTase production was optimized using the combination of Plackett-Burman experimental design (PBD) and Box-Behnken design-response surface methodology (BBD-RSM). The hydrolysis and cyclization properties of γ-CGTase were detected under the standard assay conditions with buffers of various pHs and different reaction temperatures. In enzymology, a cyclomaltodextrin glucanotransferase (also cyclodextrin glycosyl transferase or CGTase for short) (EC 2.4.1.19) is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond. Production of cyclodextrin glycosyltransferase (CGTase) is influenced by the reaction of the CGTase-producing strain towards various types of substrates.

29 Jul 2015 Cyclodextrins (CDs) are carrier molecules produced by cyclization of α-1,4- glucans by Cyclodextrin Glycosyl Transferase (CGTase). These torus  25 Oct 2010 convert starch and related substrates into cyclodextrins. (CDs) (Ishii et al., 2000). The production of CD that was catalysed by CGTase are in the  15 Jul 2014 throughout to prevent inactivation of CGTase production organism. This was analyzed in order to isolate strains of. CGTase producing bacteria.
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In this study, directed evolution was used to create three point mutants (I631T, I641T and K647E) that were produced in E. coli with shake-flask yields 1.7-, 2.1-, and 2.2-fold higher than that of wild-type The concentration of yeast extract in the medium is the most important variable for production of CGTase because it is rich in amino acids, trace elements and inorganic salts 26.The combination with 1.5% was used to achieve high CGTase activity at shorter period of cultivation. A low level (0.75%) of nitrogen source was also reported as the CGTase from B. macerans initially favors α-CD production; only in later stages of the reaction does the yield of β-CD approximate or exceed that of its α-homolog. Keywords Activate Charcoal Conversion Reaction Azeotropic Distillation Debranching Enzyme Guest Compound Cyclodextrin glycosyltransferase (CGTase) catalyzes starch conversion into cyclic or linear oligosaccharides, important industrial products for the complexation of non-polar substances. In this work, conditions to increase CGTase production from Bacillus circulans strain DF 9R were optimized by two systems.

CGTases differ in the amount and types of CDs produced. In addition, CGTase production is highly dependent on the strain, medium composition and culture conditions.
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A CGTase with high coupling activity using γ-cyclodextrin

This was analyzed in order to isolate strains of.