Abstract
Bovine skin was incubated with plant enzymes bromelain (B) and zingibain (Z) at the level of 0, 5, 10, 15, 20 and 25 unit/g of skin and gelatin was extracted at 60°C for 6h. Control gelatin was extracted without enzymatic pretreatment. The yield and gel strength were 17.90% and 283.35g for the control samples and 22.26% and 160.88g for B20 samples. The zingibain extracted gelatin (GEZ) samples failed to form gel. Viscosities of GEZ gelatins were significantly (P < 0.05) lower than the gelatins extracted using bromelain (GEB). β and α chains were absolutely degraded in all GEB and GEZ samples. Only smear bands were observed in GEZ gelatins whereas GEB samples revealed presence of low molecular weight polypeptides. Loss of molecular order was noticed in Z5 as elaborated by Fourier transform infrared (FTIR) spectroscopy. Larger particle size, denser and inter-connected irregular network was observed in B20 under scanning electron microscopy. Based on the results obtained, bromelain, particularly at level 20, could be used to obtain a better quality gelatin with higher yield compared to zingibain.
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