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A CGTase with high coupling activity using γ-cyclodextrin

The enzymes from the α-amylase family all share a similar α-retaining catalytic mechanism but can have different reaction and product specificities. One family member, cyclodextrin glycosyltransferase (CGTase), has an uncommonly high transglycosylation activity and is able to form cyclodextrins. We have determined the 2.0 and 2.5 Å X-ray structures of E257A/D229A CGTase in complex with One family member, cyclodextrin glycosyltransferase (CGTase), has an uncommonly high transglycosylation activity and is able to form cyclodextrins. 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.

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. Cell growth and CGTase synthesis in SSC using SIFR as substrate was excellent, with CGTase activity of 32,776 U g (SIFR) −1. 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 %).

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In this paper, we report an one step gel Estimation of CGTase Activity CGTase activity was measured using phenolphthalein β-cyclodextrin complexation method20. Enzyme solution dialyzed against buffer before enzyme assay. When required, different salts such as NaCl, KCl, CaCl2 and NH4Cl were introduced in the reaction mixture in 10-70 mM final The extracellular β-CGTase activity of CGTd4 reached 571.2 U/mL after 57.5 h of fermentation (Fig.

Agricultural and Biotechnological Potential of Bacillus Subtilis

Both enzymes also hydrolyzed α-, β-, and γ-cyclodextrin. Very interestingly, AmyA, but not AmyB, displayed high transglycosylation activity on maltooligosaccharides and also had significant β-cyclodextrin glycosyltransferase (CGTase) activity. CGTase activity has not been reported for typical α-amylases before.

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. The specific activity of the CGTase was increased approximately 274-fold, from 0.21 U/mg protein in crude broth to 57.7 U/mg protein after applying the DEAE-cellulose column chromatography. α-CGTase activity assay.
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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.

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.
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Cell growth and CGTase synthesis in SSC using SIFR as substrate was excellent, with CGTase activity of 32,776 U g (SIFR) −1.