CD Skripsi
Hidrolisis Kolagen Dari Kulit Ikan Gabus (Channa striata) Dengan Enzim Papain Konsentrasi Berbeda
This study aimed to determine the effect of different concentrations of papain enzyme on the characteristics of snakehead fish skin collagen and to identify the optimal concentration of papain enzyme for hydrolysis snakehead fish skin collagen. This research used an experimental method with a non-factorial Completely Randomized Design (CRD), consisting of three treatment levels: papain enzyme concentrations of 7%, 10%, and 13%. The analysis parameters included yield, moisture content, ash content, protein content, and identification of functional groups using Fourier transform infrared (FTIR) spectroscopy. The results showed that collagen extracted from snakehead fish skin (Channa striata) using various concentrations of papain enzyme (7%, 10%, and 13%) produced yields of 27.8%, 29.44%, and 31.41%, respectively. The chemical characteristics of collagen extracted with various enzyme concentrations (7%, 10%, and 13%) showed moisture content of 8.06-12.15%, ash content of 8.33-9.65%, and protein content of 31.55-53.87%, respectively. Identification of functional groups in snakehead fish skin collagen hydrolysis using different concentrations of papain enzyme showed absorption peaks in the amide absorption region, including amide A, amide B, amide I, amide II, and amide III, which are typical of collagen absorption. The optimal papain enzyme concentration was determined to be 13%, which yielded collagen with characteristics of 31.41% yield, 8.06% moisture content, 8.33% ash content, and 53.87% protein content.
Keywords: collagen, extraction, skin , snakehead fish, papain enzyme.
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