Developing a Fish Meat‐binding Agent: Purification of Salmon Thrombin

• Published in: Journal of Food Science
• Main Authors: Manseth, E., Skjervold, P.O., Flera, S.O., Brosstad, F.R., ØDegaard, O.R., Flengsrud, R.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2003
• Subjects: Atlantic salmon; Salmo salar
• Online Access: http://dx.doi.org/10.1111/j.1365-2621.2003.tb12307.x; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2621.2003.tb12307.x; http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2621.2003.tb12307.x/fullpdf

ABSTRACT Thrombin from Atlantic salmon ( Salmo salar ) was purified and characterized as a potential new binding agent for the food industry. Purification was performed avoiding inhibitors, using BaSO 4 adsorption and heparin‐Sepharose affinity chromatography. Prothrombin activation was performed using a mixture of eggs and gills from salmon. Optimized conditions for the adsorption, elution, and the activation step are presented. The purified thrombin clotted bovine fibrinogen with a specific activity of 1423 U/mg. Sequence data are presented and compared with other species. This method of nontoxic activation and purification will allow salmon thrombin to be used in the food industry.