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- W2023667342 abstract "The ring-opening metathesis polymerization (ROMP) of norborn-2-ene (NBE) and cis-cyclooctene (COE) was initiated with well-defined Grubbs-type initiators, i.e., RuCl2(CHPh)(PCy3)2 (1), [RuCl2(PCy3)(IMesH2)(CHPh)] (2), and [RuCl2(3-Br-Py)2(IMesH2)(CHPh)] (3) (MesH2 = 1,3-bis(2,4,6-trimethylphenyl)imidazolin-2-ylidene, PCy3 = tricyclohexylphosphine, 3-Br-Py = 3-bromopyridine). Reaction of the living polymers with O2 (air) resulted in the formation of aldehyde−semitelechelic polymers in up to 80% yield, depending on the initiator and monomer used. To proof aldehyde formation, the terminal aldehyde groups were converted into the corresponding 2,4-dinitrophenylhydrazine derivatives, and the structure of the hydrazones was confirmed by NMR and IR spectroscopy. This simple methodology was then used for the functionalization of ROMP-derived monoliths prepared from NBE, 1,4,4a,5,8,8a-hexahydro-1,4,5,8-exo-endo-dimethanonaphthalene (DMN-H6) and (NBE-CH2O)3SiCH3, to yield aldehyde-funtionalized monoliths. The extent of aldehyde formation was determined by hydrazone formation. Up to 8 μmol of aldehyde groups/g monolith could be generated by this approach. Finally, these aldehyde-functionalized monoliths were used for the immobilization of trypsin. Excellent proteolytic activity of the immobilized enzyme was found both under batch and continuous flow conditions." @default.
- W2023667342 created "2016-06-24" @default.
- W2023667342 creator A5015498267 @default.
- W2023667342 creator A5016791337 @default.
- W2023667342 date "2010-11-16" @default.
- W2023667342 modified "2023-09-27" @default.
- W2023667342 title "A Continuous Bioreactor Prepared via the Immobilization of Trypsin on Aldehyde-Functionalized, Ring-Opening Metathesis Polymerization-Derived Monoliths" @default.
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- W2023667342 doi "https://doi.org/10.1021/ma101922s" @default.
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