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Developing a Fish Meat‐binding Agent: Purification of Salmon Thrombin
Author(s) -
Manseth E.,
Skjervold P.O.,
Flera S.O.,
Brosstad F.R.,
ØDegaard O.R.,
Flengsrud R.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb12307.x
Subject(s) - thrombin , salmo , chemistry , affinity chromatography , adsorption , fibrinogen , sepharose , fish <actinopterygii> , elution , chromatography , coagulation , biochemistry , fishery , biology , enzyme , organic chemistry , immunology , platelet , psychology , psychiatry
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.