Summary
A new HPLC stationary phase was synthesized by the covalent immobilization of the enzyme trypsin (TRYP) on silica. The hydrolytic activity of the immobilized enzyme was 72% of the activity of an equivalent molar amount of free TRYP. The initial chromatographic studies indicate that this phase can be used for chiral separations of enantiomeric O- and N,O-derivatized amino acids which are natural substrates on TRYP and that the stereochemical resolutions are a result of the activity of the enzyme.
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Thelohan, S., Jadaud, P. & Wainer, I.W. Immobilized enzymes as chromatographic phases for HPLC: The chromatography of free and derivatized amino acids on immobilized trypsin. Chromatographia 28, 551–555 (1989). https://doi.org/10.1007/BF02260675
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DOI: https://doi.org/10.1007/BF02260675