14101-61-2Relevant academic research and scientific papers
SEPARATION OF CHIRAL ISOMERS BY SFC
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Page/Page column 35, (2016/12/22)
The present invention relates to the field of separating chiral isomers from each other. Particularly, it relates to the field of separating of chiral isomers of chromane or chromene compounds, particularly tocopherols, 3,4-dehydro-tocopherols and tocotrienols, as well as the protected forms thereof. It has been found that the use of supercritical carbon dioxide as mobile phase combined with the very specific chiral phase as stationary phase leads to a very efficient separation of the individual chiral isomers. As the method is very efficient and fast combined with advantageous in view of ecology it is of big industrial interest.
A short and convenient chemical route to optically pure 2-methyl chromanmethanols. Total asymmetric synthesis of β-, γ-, and δ-tocotrienols
Couladouros, Elias A.,Moutsos, Vassilios I.,Lampropoulou, Maria,Little, James L.,Hyatt, John A.
, p. 6735 - 6741 (2008/02/11)
(Chemical Equation Presented) With use of inexpensive commercially available raw materials, chromanmethanol precursors to the natural β-, γ-, and δ-tocotrienols have been prepared in high yield. Enzymatic resolution afforded chiral chromanmethanols in high enantiomeric excess. Subsequent attachment of the farnesyl side chain was high yielding, thus allowing the preparation of asymmetric β-, γ-, and δ-tocotrienols in one final step wherein simultaneous deprotection of the phenol and removal of the sulfone group occurs. This chemistry provides the first synthesis of natural-series β-tocotrienol.
The substrate specificity of tocopherol cyclase
Stocker, Achim,Fretz, Heinz,Frick, Haroun,Ruettimann, August,Woggon, Wolf-Dietrich
, p. 1129 - 1134 (2007/10/03)
The substrate specificity of the enzyme tocopherol cyclase from the blue-green algae Anabaena variabilis (Cyanobacteria) was investigated with 11 substrate analogues revealing the significance of three major recognition sites: (i) the OH group at C(1) of the hydroquinone, (ii) the (E) configuration of the double bond, and (iii) the length of the lipophilic side chain. Experiments with two affinity matrices suggest that substrates approach the enzyme's active site with the hydrophobic tail.
