BibTex Citation Data :
@article{JAFT40–43, author = {Sri Mulyani and Umar Santoso and Yudi Pranoto and Francis Setyabudi and Anang Legowo}, title = {The Functional Properties of Buffalo skin Gelatin Extracted Using Crude Acid Protease from Cow’s Abomasum}, journal = {Journal of Applied Food Technology}, volume = {6}, number = {2}, year = {2019}, keywords = {buffalo skin gelatin, emulsion activity index, emulsion stability, foaming expansion, foaming stability.}, abstract = { The study was investigated the functional properties of buffalo skin gelatine. Gelatine was extracted from swamp buffalo skin using crude acid protease from cow’s abomasum (CAPC) in concentration variation 0; 2.5; 5; and 7.5 U/mg. The temperature to hydrolysis included at 28 °C, 37°C and 40°C. The emulsion activity index (EAI), Emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS) were investigated. The interaction between CAPC concentration and hydrolysis temperature has a significant effect (P <0.05) on the emulsion activity index (EAI), emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS). The highest EAI was obtained in CAPC concentration of 5 U /mg, hydrolysis temperature of 40°C, which was 12.04 m2/g. The higher concentration of CAPC decreased the ESI. The hydrolysis temperature of 40°C produces higher FE than 28°C and 40°C. The highest FE is obtained at CAPC 5U/mg, 37°C hydrolysis temperature, which is 102.93%. The FS values range from 44.91-55.00%. This value is higher than commercial gelatin (bovine skin gelatin) which is 34.90%. The conclusion of this study is that buffalo skin gelatin with the best functional properties was obtained using CAPC 5 U/mg, the hydrolysis temperature of 40°C. }, issn = {2614-7076}, doi = {10.17728/jaft.6464}, url = {https://ejournal2.undip.ac.id/index.php/jaft/article/view/40%E2%80%9343} }
Refworks Citation Data :
The study was investigated the functional properties of buffalo skin gelatine. Gelatine was extracted from swamp buffalo skin using crude acid protease from cow’s abomasum (CAPC) in concentration variation 0; 2.5; 5; and 7.5 U/mg. The temperature to hydrolysis included at 28 °C, 37°C and 40°C. The emulsion activity index (EAI), Emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS) were investigated. The interaction between CAPC concentration and hydrolysis temperature has a significant effect (P <0.05) on the emulsion activity index (EAI), emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS). The highest EAI was obtained in CAPC concentration of 5 U /mg, hydrolysis temperature of 40°C, which was 12.04 m2/g. The higher concentration of CAPC decreased the ESI. The hydrolysis temperature of 40°C produces higher FE than 28°C and 40°C. The highest FE is obtained at CAPC 5U/mg, 37°C hydrolysis temperature, which is 102.93%. The FS values range from 44.91-55.00%. This value is higher than commercial gelatin (bovine skin gelatin) which is 34.90%. The conclusion of this study is that buffalo skin gelatin with the best functional properties was obtained using CAPC 5 U/mg, the hydrolysis temperature of 40°C.
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