A chemoenzymatic route to chiral siloxanes

An approach employing two enzymes—toluene dioxygenase and immobilized lipase B from Candida antarctica (N435)—was explored as a potential biocatalytic method for the coupling of chiral diols with siloxane species. Analysis of reaction mixtures using1H NMR spectroscopy suggested that up to 66% consum...

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Bibliographic Details
Published in:Tetrahedron
Main Authors: Naoum, Ravi, Séguin, Jacqueline P., Trant, John F., Frampton, Mark B., Hudlický, Tomáš, Zelisko, Paul M.
Format: Text
Language:unknown
Published: Scholarship at UWindsor 2016
Subjects:
Biotransformations
Chemoenzymatic
Chirality
Siloxane
Transesterification
Biochemistry
Biophysics
and Structural Biology
Chemistry
Antarc*
Antarctica
Online Access:https://scholar.uwindsor.ca/chemistrybiochemistrypub/211
https://doi.org/10.1016/j.tet.2016.05.032
https://scholar.uwindsor.ca/context/chemistrybiochemistrypub/article/1213/viewcontent/21_Toward_the_Chemoenzymatic_Synthesis_of_Chiral_Siloxane_Polymers___Accepted.pdf
Description
Summary:An approach employing two enzymes—toluene dioxygenase and immobilized lipase B from Candida antarctica (N435)—was explored as a potential biocatalytic method for the coupling of chiral diols with siloxane species. Analysis of reaction mixtures using1H NMR spectroscopy suggested that up to 66% consumption of the siloxane starting materials had occurred. Oligomeric species were observed and chiral products from the coupling of a cyclic diol with a siloxane molecule were isolated and characterized by MALDI-ToF MS and GPC. Immobilized lipases from Rhizomucor miehei and Thermomyces lanuginosus were also explored as potential catalysts for the coupling reactions, however, their use only returned starting material.

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