Developing a Fish Meat-binding Agent: Purification of Salmon Thrombin |
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| Authors: | E Manseth PO Skjervold SO Flera FR Brosstad OR Ødegaard R Flengsrud |
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| Affiliation: | Authors Manseth and Flengsrud are with the Dept. of Chemistry and Biotechnology, Agricultural Univ. of Norway, 1430 Ås, Norway. Authors Skjervold and Fjaera are with the Dept. of Agricultural Engineering, Agricultural Univ. of Norway, Ås, Norway. Author Brosstad is with the Research Inst. for Internal Medicine, Univ. of Oslo, Oslo, Norway. Author Ødegaard is with the Dept. of Clinical Chemistry, Aker Univ. Hospital, Oslo, Norway. Direct inquiries to author Manseth (Email: ). |
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| 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 BaSO4 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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| Keywords: | thrombin salmon heparin-affinity fibrinogen meat binding |
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