For specific applications, it is highly dependent upon its physico-chemical features that are highly affected by species and tissue extracted and extraction method. Gelatin quality is mostly dependent upon the rheological properties, particularly the gel strength and viscosity, but other characteristics, especially transparence, presence of color and smell and solubility, are also important. In food industry, gelatin is one of the water-soluble polymers that can be used as materials to raise the food elasticity, consistence, and stability. It could also be used for diabe- tics and can reduce body weight. It is mostly applied as stabilizer, gelling, fastener, emulsifier, adhesive, and edible food wrapping. Gelatin is mainly used in food, pharmaceutical, medical, cosmetic and photographic industries and has unique physical and chemical properties. Introduction Gelatin is a fibrous protein produced through thermal denaturation or collagen partial degradation of animal bone and skin. As conclusion, the extraction process modification using the whiting could increase the skin gelatin properties of the pangas catfish ( Pangasius pangasius), and the fish skin is a prospective source of good gelatin with desired functional properties.ġ. SEM micrographs also showed that the catfish gelatin pre-treated with the whiting had thick strand with small voids and dense tissue. The gelatin SDS-PAGE with pre-treatment of whiting (CaO) was 136.56 kDa, and the rheological test exhibited higher elastic modulus (G’) and viscous modulus (G”) than that of other treatments and commercial gelatin. The high viscosity, gelling temperature, and melting temperature were 7.87 (cP), 18.67℃, and 31.67℃, respectively. High gelatin (dry basis) was 23.37% and gel strength was 360.18 g. The preliminary treatment using the whiting solution gave higher gelatin property (P<0.05) than that using alum (Al 3(SO 4) 2) and Calcium Hydroxide (Ca(OH) 2). These levels are generally assumed to be safe for fish-allergic individuals.This study was aimed at studying the effect of preliminary treatment variations on the pangas catfish ( Pangasius pangasius) skin gelatin, particularly the gel strength. From the other 22 lots, the one with the highest concentration contained 0.15 µg g(-1) of parvalbumin. From 95 commercial lots of fish gelatin it is shown that 73 are below 0.02 µg g(-1) parvalbumin. Washing of the skins, a common industrial procedure during the manufacturing of fish gelatin, reduced the level of parvalbumin about 1000-fold to 0.5 µg g(-1), or 0.5 ppm. The data show that the parvalbumin content in cod muscle tissue is 6.25 mg g(-1), while the skins contained considerably less, 0.4 mg g(-1). Fish gelatin, wine and beer, matrices for the potential use of this ELISA, did not cause disturbance of the assay performance. The ELISA was sufficiently sensitive (LLOQ = 0.8 ng ml(-1) in extracts, corresponding to 0.02 µg of parvalbumin per g of tissue), and did not cross-react with common food constituents. The ELISA was applied to measure parvalbumin in cod skin, the starting material for fish gelatin made from deep sea, wild fish. The antibodies were tested for specificity and an enzyme-linked immunosorbent assay (ELISA) was developed using these antibodies. The major allergen parvalbumin was purified from cod muscle tissues, and polyclonal antibodies were raised towards it.
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