| 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.
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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,