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Engineered cyclodextrin glucanotransferases from Bacillus sp. G-825-6 produce large-ring cyclodextrins with high specificity.
Engineered cyclodextrin glucanotransferases from Bacillus sp. G-825-6 produce large-ring cyclodextrins with high specificity.
- Source :
-
MicrobiologyOpen [Microbiologyopen] 2019 Jun; Vol. 8 (6), pp. e00757. Date of Electronic Publication: 2018 Oct 25. - Publication Year :
- 2019
-
Abstract
- Cyclodextrin glucanotransferases (CGTases) synthesize cyclic oligosaccharides (cyclodextrins, CD) from starch. A CGTase from Bacillus sp. G-825-6 was engineered by site-directed mutagenesis at two positions by the construction of the variants Y183W, Y183R, D358R, Y183W/D358R, and Y183R/D358R. Among CD composed of 7-12 glucose units (CD7-CD12), Y183W mainly produced CD8. Y183R had completely lost its ability to synthesize CD7, and CD8 and the larger CD were the only cyclic oligosaccharides produced. D358R also formed mainly CD8-CD12 during a reaction time of 24 hr. The double mutant Y183W/D358R showed combined characteristics of the single mutations with very low CD7 cyclization activity and an increased formation of the larger CD. The results show that CGTases synthesizing mainly CD8-CD12 can be constructed allowing a convenient production of larger CD in significant amounts as host molecules in supramolecular complexing reactions.<br /> (© 2018 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.)
- Subjects :
- Bacillus genetics
Bacillus metabolism
Bacterial Proteins metabolism
Cyclodextrins chemistry
Glucosyltransferases metabolism
Mutagenesis, Site-Directed
Protein Engineering
Substrate Specificity
Bacillus enzymology
Bacterial Proteins chemistry
Bacterial Proteins genetics
Cyclodextrins metabolism
Glucosyltransferases chemistry
Glucosyltransferases genetics
Subjects
Details
- Language :
- English
- ISSN :
- 2045-8827
- Volume :
- 8
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- MicrobiologyOpen
- Publication Type :
- Academic Journal
- Accession number :
- 30358941
- Full Text :
- https://doi.org/10.1002/mbo3.757