| Summary: | Pepsin enzyme was used to pretreat the bovine skin at the rate of 5, 15, and 25 units of enzyme/g of skin to recover gelatin, and the recovered gelatins were referred to as Pe5, Pe15, and Pe25, respectively. The gelatin yield increased significantly (p < 0.05) from 18.17% for Pe5 to 24.67% for Pe25 as the level of pepsin increased, but the corresponding gel strength and viscosity decreased significantly (p < 0.05) from 215.49 to 56.06 g and 9.17 to 8.17 mPa center dot s for Pe5 and Pe25, respectively. beta- and alpha 1- and alpha 2-chains were degraded entirely in all the gelatins samples as observed in protein pattern elaborated by gel electrophoresis. H-1 nuclear magnetic resonance (H-1 NMR) analysis indicated the coiled structure of gelatin protein chains. The lowest amide III amplitude of Pe25 as found by Fourier transform infrared (FTIR) spectroscopy indicated that alpha-helix structure of protein chains were lost to more irregular coiled structure. Thus, it could be summarized that pepsin might be used at the lower level (5 units/g of wet skin) to extract gelatin from bovine skin with good functional properties and at higher level (15/25 units/g of wet skin) to obtain gelatin of industrial grade with high yield.
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