Gelatin, a protein derived from collagen, is widely used in food, pharmaceutical, and cosmetic industries. The use of conventional porcine-derived gelatin raises concerns about halal compliance, highlighting the need to develop alternative gelatin sources acceptable to a broader range of consumers. This study successfully produced halal gelatin from goat skin through enzymatic extraction using a mixture of proteases produced by indigenous bacterial isolates MSF6 and MSF11. Optimal protease production was achieved on day 2 at pH 9 and 37 °C, while maximum protease activity was observed at pH 9 and 57 °C. The highest gelatin recovery (78.93%) was obtained using a 3:1 ratio of crude protease extracts from MSF6 and MSF11. ATR-FTIR analysis revealed characteristic amide A and amide I absorption bands, while SDS-PAGE analysis showed a predominant protein band with a molecular weight of 66.34 ± 2.65 kDa. The extracted gelatin exhibited a gelling temperature of 8 °C, a pH of 7.56, and a gel strength of 19.9 Bloom.
Copyrights © 2026