Suharti Suharti
Departemen Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam, Universitas Negeri Malang

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Enzymatic Extraction of Gelatin from Goat Skin Using Combined Proteases from Indigenous Bacterial Isolates MSF6 and MSF11 Fanny Anggita Febrianingrum; Mieke Alvionita; Intan Kusuma Dewi; Suharti Suharti
JC-T (Journal Cis-Trans) : Jurnal Kimia dan Terapannya Article in Press
Publisher : Universitas Negeri Malang

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Abstract

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.
Optimization Of Keratinase Production and Characterization By Bacterial Isolates MSF6 And MSF11 Putri Kurnia; Mieke Alvionita; Intan Kusuma Dewi; Suharti Suharti
JC-T (Journal Cis-Trans) : Jurnal Kimia dan Terapannya Vol. 9 No. 2 (2025)
Publisher : Universitas Negeri Malang

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.17977/um0260v9i22025p032

Abstract

Chicken feather waste is a major environmental issue in Indonesia, with an estimated 189 million kg generated by 2024 due to high poultry consumption. Composed of approximately 90% keratin, chicken feathers represent a promising substrate for bioconversion into value-added products using keratinase. This study aimed to optimize keratinase production and characterize the enzyme produced by two indigenous bacterial isolates, MSF6 and MSF11, obtained from chicken slaughterhouse soil. Laboratory experiments included the optimization of fermentation conditions (pH and temperature), enzyme activity assays, and feather degradation tests. Optimal enzyme production was achieved at pH 9 and 37°C, whereas maximum enzyme activity was observed at pH 10 and 62°C. The combined keratinase preparation (MSF6 = 3:2) exhibited the highest degradation efficiency, yielding 277.62 µg/mL of soluble protein and a 17% reduction in feather weight. These findings highlight the potential of indigenous bacteria for the sustainable management and valorization of chicken feather waste.