Abstract
Gelatin from bighead carp (Hypophthalmichthys nobilis) scale was extracted with the gel strength of 415.7 ± 9.9 g. Ammonium sulfate fractional precipitation (ASFP) with different ammonium sulfate saturations (20%, 25%, 30%, 35% and 40%, respectively) separated fish gelatin components with different gel strengths (469.7 ± 12.0 g, 419.7 ± 9.9 g, 181.9 ± 17.7 g, 83.9 ± 9.9 g and 15.3 ± 2.1 g, respectively). ASFP did not destroy characteristic FTIR peaks (amide A, amide I, amide II and amide III) and X-ray diffraction peaks (around 7° and 20–21° represented the triple-helix structure and the single left-hand helix chain, respectively) in the fish gelatin. In addition, lower ammonium sulfate saturation precipitated the fish gelatin component with stronger hydrogen bond, more triple-helix structures, higher molecular weight distribution and denser microstructure. Prominently, fish gelatin with higher gel strength had greater amount of high molecular weight components and denser microstructure.
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