Heat-extracted bovine lung gelatin contained predominantly collagen γ– chains, β– chains and α– chains (α1(I) and α2(I)), with some low molecular weight peptides, while the pepsin-extracted lung gelatins were characterized by comparatively decreased β– and α– chains and increased low molecular weight peptides. Increased imino acid (proline and hydroxyproline) content was associated with increased gelling and melting temperatures and was comparable to commercial bovine gelatin. Gel strengths of bovine lung gelatin were comparable to or lower than and foam stability and emulsifying activity were lower than commercial bovine gelatin. Transmittance of bovine lung gelatin was substantially reduced compared to that of commercial bovine gelatin but had increased water and fat-binding capacity, and comparable or increased gelling and melting temperature. Bovine lung gelatin had pH, moisture and protein comparable to or less than that of commercial bovine gelatin and decreased ash. All bovine lung gelatin contained protein as the major proximate component, with little ash and non-detectable fat. Pepsin increased gelatin yield by about 9-fold that of heat extraction alone. Gelatin from bovine lungs was extracted using heat and pepsin and the resulting gelatins were characterized. ![]() Gelatin is extracted from animal tissues using heat usually with low yields, but pepsin may increase high quality gelatin yield per unit of tissue.
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