Rifqi, Rifqi and Jamhari, Jamhari and Erwanto, Y. (2020) Isolation and characterization of collagen from local goat bone using pepsin hydrolysis. In: 2nd International Conference of Animal Science and Technology, ICAST 2019 Makassar 5 November 2019.
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Rifqi_2020_IOP_Conf._Ser.__Earth_Environ._Sci._492_012083.pdf
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Abstract
Goat bone is one of by-product which has not commonly used in Indonesia. Collagen is one of proteins which contained a bone which characterizing its uniq function. The purpose of experiment was to isolate and characterize collagen from local goat bone with pepsin enzymatic hydrolysis in various concentration. The experiment consisted of bone preparation, Isolating by leaching method, and the hydrolysis of collagen bone using pepsin enzyme in various concentration (0.1; 0.3; 0.5; and 1). Variables observed were collagen yield, soluble protein, pH, Fourier Tansform Infrared Spectroscopy (FTIR) spectra, thermal stability using Differential Scanning Calorimetry (DSC), and molecular weight using Sodium Dodesyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). The results showed that soluble protein concentration of collagen solution was not affected by pepsin concentrations. The soluble protein of 0.1; 0.3; 0.5 and 1 of enzym were 0.2030,013; 0.2440,045; 0.2950,065; and 0.2570,066 mg/ml for, respectively. The results of collagen yield was significant, and it were 7.12; 7.54; 13.3; dan 8.81 . The results of pH showed significant, it was 6.37; 5.96; 6.88; 5.92. The FTIR spectra showed that all of the sample has not changed into gelatin. The thermal stability in DSC analysis showed that the collagen start to gelation at 56.72 to 57.40 C and Tmax for each sample were 128.20; 189.32; 131.35; 124.43 C, respectively. In conclusion, collagen could be isolated from goat bone using enzymatic treatment and showed the fine properties as well as collagen from skin. © Published under licence by IOP Publishing Ltd.
Item Type: | Conference or Workshop Item (Paper) |
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Additional Information: | Cited by: 2; All Open Access, Gold Open Access |
Uncontrolled Keywords: | Animals; Collagen; Differential scanning calorimetry; Electrophoresis; Fourier transform infrared spectroscopy; Gelation; Sodium compounds; Sulfur compounds; Thermodynamic stability; Collagen yield; Enzymatic treatments; FT-IR spectrum; Indonesia; Isolation and characterization; Leaching methods; Polyacrylamide gel electrophoresis; Soluble proteins; Enzymatic hydrolysis |
Subjects: | S Agriculture > SF Animal culture |
Divisions: | Faculty of Animal Sciences > Department of Animal Products Technology |
Depositing User: | Sri JUNANDI |
Date Deposited: | 17 Feb 2025 07:38 |
Last Modified: | 17 Feb 2025 07:38 |
URI: | https://ir.lib.ugm.ac.id/id/eprint/14218 |