Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10542013 | Food Chemistry | 2012 | 10 Pages |
Abstract
⺠Purification of a chymotrypsin from the hepatopancreas of cuttlefish (Sepia officinalis). ⺠The molecular weight of the purified chymotrypsin was estimated to be 28 kDa by SDS-PAGE. ⺠The optimum pH and temperature for chymotrypsin activity were around 8.5 and 55 °C, respectively. ⺠The enzyme was extremely stable in the pH range of 7.0-10.0 and highly stable up to 50 °C after 1 h incubation. ⺠The N-terminal amino acid sequence of the first 20 amino acids of the purified chymotrypsin was IVGGQEATIGEYPWQAALQV.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Rafik Balti, Fateh Bougherra, Ali Bougatef, Ben Khaled Hayet, Naima Nedjar-Arroume, Pascal Dhulster, Didier Guillochon, Moncef Nasri,