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Tuning the Outcome of Enzyme‐Mediated Dynamic Cyclodextrin Libraries to Enhance Template Effects
Author(s) -
Larsen Dennis,
Beeren Sophie R.
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202001076
Subject(s) - cyclodextrin , chemistry , glycosidic bond , enzyme , combinatorial chemistry , solvent , organic chemistry
Abstract Enzyme‐mediated dynamic combinatorial chemistry combines the concept of thermodynamically controlled covalent self‐assembly with the inherent biological relevance of enzymatic transformations. A system of interconverting cyclodextrins has been explored, in which the glycosidic linkage is rendered dynamic by the action of cyclodextrin glucanotransferase (CGTase). External factors, such as pH, temperature, solvent, and salinity are reported to modulate the composition of the dynamic cyclodextrin library. Dynamic libraries of cyclodextrins (CDs) could be obtained in wide ranges of pH (5.0–9.0), temperature (5–37 °C), and salinity (up to 7.5 m NaNO 3 ), and with high organic solvent content (50 % by volume of ethanol), showing that enzyme‐mediated dynamic systems can be robust and not limited to physiological conditions. Furthermore, it is demonstrated how strategic choice of reaction conditions can enhance template effects, in this case, to achieve highly selective production of α‐CD, an otherwise challenging target due to competition from the structurally similar β‐CD.