Comparative characteristics of chymotrypsin covalently bound on chemically and enzymatically oxidized agaroses

Autor:	Kamen Voivodov, Nikolina Stambolieva, Jaroslava Turková
Rok vydání:	1991
Předmět:	chemistry.chemical_classification Chymotrypsin Immobilized enzyme biology Stereochemistry Applied Microbiology and Biotechnology Biochemistry Combinatorial chemistry Aldehyde chemistry.chemical_compound Enzyme chemistry Covalent bond biology.protein Agarose Titration
Zdroj:	Biotechnology Techniques. 5:219-222
ISSN:	1573-6784 0951-208X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::77d7add90bc0b9bb28f9516439bb85ee https://doi.org/10.1007/bf00152785 Zobrazit plný text záznamu Full text from SpringerLink