Immobilization of α‐chymotrypsin and trypsin on different agarose gels

Autor:	S.F. Gauthier, Jean-Christophe Vuillemard, N. Lizotte
Rok vydání:	1991
Předmět:	chemistry.chemical_classification Chymotrypsin Chromatography biology Immobilized enzyme Trypsin Applied Microbiology and Biotechnology Enzyme assay Sepharose Colloid chemistry.chemical_compound Enzyme chemistry biology.protein medicine Agarose Food Science Biotechnology medicine.drug
Zdroj:	Food Biotechnology. 5:105-117
ISSN:	1532-4249 0890-5436
DOI:	10.1080/08905439109549796
Popis:	Four preactivated agarose gels were evaluated with two proteases, α‐chymotrypsin and trypsin, for the amount of protein and active enzyme immobilized. CNBr‐Activated Sepharose 4B was found to be the best among the four gels tested since it gave the highest amount of active enzyme per g of gel for both α‐chymotrypsin (5.1 mg/g of gel) and trypsin (17.1 mg/g of gel). The lowest amount of active enzyme per g of gel was obtained with CNBr‐Activated Sepharose 6MB. The presence of spacer arms in Activated CH‐Sepharose 4B did not improve the coupling yields of the enzymes. When gels were lyophilized losses in enzyme activity (25–60%) were observed. In addition, CNBr‐Activated Sepharose 4B gel was resistant to abrasive treatment and lyophilization as illustrated by scanning electron micrographs.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1848978f58ca6f869d11d05139835f31 https://doi.org/10.1080/08905439109549796 Zobrazit plný text záznamu