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

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 us...

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Bibliographic Details
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
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Summary: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.

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