| Abstract: | The degree of hydrolysis of substrates attached to silica supports with alpha-chymotrypsin has been evaluated relative to the production of "internal surface reversed-phase" supports. The peptide substrates N-tert.-butoxycarbonyl-L-phenylalanine (Boc-L-Phe), N-carbobenzoxy-L-valine-L-phenylalanine, N-acetyl-L-phenylalanine (acetyl-L-Phe) and N-benzoyl-L-phenylalanine as well as phenylpropionic acid were attached to glycerylpropyl-bonded silica via a diamine spacer using 1,1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a coupling catalyst. The products released from the silica support on enzyme treatment were quantified by high-performance liquid chromatography. Boc-L-Phe and acetyl-L-Phe were successfully cleaved from the rigid silica matrix in high yields, whereas the remaining substrates were hydrolyzed to a lesser extent. |
