Abstract
This paper describes the production of the novel recombinant trypsin Y polypeptide from Atlantic cod (Gadus morhua) in a Pichia pastoris expression system and gives a characterization of the enzyme. It presents the first biochemical data supplementing the molecular description of the putative group III trypsins. Unexpectedly, the results demonstrate that the recombinant trypsin Y has a dual substrate specificity demonstrating both trypsin and chymotrypsin activities. It shows increasing proteolytic activity at temperatures between 2-21°C, and it is completely inactivated at 30°C. These properties may be important for the commercial use of recombinant trypsin Y, as other cold-adapted proteolytic enzymes from the Atlantic cod have proven their usefulness in various industrial and medical applications.
Original language | English |
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Pages (from-to) | 85-100 |
Number of pages | 16 |
Journal | Journal of Aquatic Food Product Technology |
Volume | 13 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2004 |
Other keywords
- Atlantic cod
- Cold-adapted
- Expression
- Group III trypsin
- Serine protease