We have found a fraction of proteins which is able to differentiate porcine and bovine gelatins accurately, with distinctive protein bands in SDS-PAGE at 140 kDa and 110 kDa for bovine and porcine samples, respectively. The most commonly used gelatines in those products are porcine and bovine gelatines. Sample was prepared using ammonium sulfate precipitation and subjected to gel electrophoresis for protein separation. Gelatin is soluble in glycerol and acetic acid, and more soluble in hot than in cold water.1 It is practically insoluble in most organic solvents such as alcohol, chloroform, carbon disulfide, carbon tetrachloride, ether, benzene, acetone, and oils.10 Sterile solutions of gelatin, stored cold, remain unchanged indefinitely. Abstract Background Gelatine is one of the components commonly used in food, cosmetics and pharmaceutical products due to its gelling properties. In our present study, differentiation of sources of gelatin was made possible in a simplified yet economical method. Due to these reasons, differentiation of the source of gelatins has been very difficult. Nevertheless, these different origins of gelatin have much similarity in term of structures, physicochemical properties and amino acid sequences. The source of gelatins is usually from porcine and bovine, and less commonly from vegetable and fish. Gelatin is commonly used in food supplements and in the form of soft or hard capsules.
0 kommentar(er)
