Summary
The enzymatically activated agaroses compared with chemically activated show 25 fold lower amount of generated aldehyde groups, 33 fold lower binding capacity for chymotrypsin, 3 fold lower proteolytic as well as amidolytic activity toward AntAlaAlaPheNA of the corresponding fixed enzyme. Trans-cinnamoylimidazole titration data demonstrate 100% active bound enzyme in the case of enzymatically oxidized agaroses and 57% for chemically oxidized. The enzymic activation offers a small number of sites for ligand attachment in a unique microenvironment. The chemical activation yields a suitable matrix for effective chymotrypsin immobilization.
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Voivodov, K., Stambolieva, N. & Turkova, J. Comparative characteristics of chymotrypsin covalently bound on chemically and enzymatically oxidized agaroses. Biotechnol Tech 5, 219–222 (1991). https://doi.org/10.1007/BF00152785
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DOI: https://doi.org/10.1007/BF00152785