JAFT • pISSN 2355-9152 • eISSN 2614-7076 • Member of CrossRef®
skip to main content

The Functional Properties of Buffalo skin Gelatin Extracted Using Crude Acid Protease from Cow’s Abomasum

*Sri Mulyani  -  Department of Food Technology, Faculty of Animal and Agricultural Sciences, Diponegoro University, Indonesia, Indonesia
Umar Santoso  -  Faculty of Agricultural Technology, Gadjah Mada University, Indonesia, Indonesia
Yudi Pranoto  -  Faculty of Agricultural Technology, Gadjah Mada University, Indonesia, Indonesia
Francis M.C. Setyabudi  -  Faculty of Agricultural Technology, Gadjah Mada University, Indonesia, Indonesia
Anang Mohamad Legowo  -  Department of Food Technology, Faculty of Animal and Agricultural Sciences, Diponegoro University, Indonesia, Indonesia
Open Access Copyright 2019 Journal of Applied Food Technology

Citation Format:
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.

Fulltext View|Download
Keywords: buffalo skin gelatin, emulsion activity index, emulsion stability, foaming expansion, foaming stability.
Funding: Diponegoro University and Gadjah Mada University

Article Metrics:

  1. Aewsiri, T., Benjakul, S., Visessanguan, W. (2009). Functional properties of gelatin from cuttlefish (Sepia pharaonis) skin as affected by bleaching using hydrogen peroxide. Food Chemistry, 115: 243−249
  2. Balti, R., Jridi, M., Sila, A., Souissi, N.,Arroume. N.N, Guillochon, D. Nasri, M. (2011). Extraction and functional properties of gelatin from the skin of cuttlefish (Sepia officinalis) using smooth bound crude acid protease- aided process. Food Hydrocolloids 25: 943-950
  3. Bkhairia, I., Mhamdi,S. Jridi, M, Nasri, M. (2016). New acidic proteases from Liza aurata: Characterization and application in gelatin production. International Journal of Biological Macromolecules 92: 533-542
  4. Bougatef, A., Balti.R, Sila.A, Nasri,R., Graia, A, Nasri, M. (2012). Recovery and physical properties of smooth hound (mustelus mustelus) skin gelatin. LWT- Food Science and Technology 48: 248-254
  5. Castillo-Yanez, F. J., Pacheco-Aguilar, R., Garcia-Carreno, F. L., Navarrete-Del Toro, M.d.L.A. (2004). Characterization of acididc proteolytic enzyme from monterey Sardine (Sardinops sagax caerulea) viscera. Journal of Food Chemistry, 85, 343-350
  6. Dickinson, E., Lorient, D. (1994). Emulsions. In E. Dickinson, D. Lorient (Eds.), Food Macromolecules and Colloids (Pp. 201–274). Cambridge, UK: The Royal Society of Chemistry
  7. Duan, R., Zhang, J., Liu, L., Cui, W., Regenstein, J. M. (2018). The Functional properties and application of gelatin derived from the skin of channel catfish (Ictalurus punctatus). Food Chemistry 239, 464–469
  8. Hasna, T., Mulyani, S., Santoso, U., Pranoto, Y.2019. Extraction of Crude Acid Protease from Goat ( Capra aegagrus ) Abomasum. 8, 2018–2019
  9. Haug, I.J., K.I.Draget. (2009). Gelatin in Handbook of Hydrocolloids. Norwegian University of Science and Technology (NTNU), Norway
  10. Jongjareonrak, A., Benjakul, S., Visessanguan, W., Bagai, T.,Tanaka, M. (2005). Isolation and characterisation of acid and pepsin-solubilised collagens from the skin of brownstripe red snapper (Lutjanus vitta). Food Chemistry, 93: 475-484
  11. Jridi, M., Nasri,,R. Ben salem, R.B.S, Lassoued,I., Barkia, A., Nasri, M Souissi.N. (2015). Chemical and biophysical properties of gelatins extracted from the skin of octopus (Octopus vulgaris). LWT - Food Science & Technology 60: 881–889
  12. Jridi, M., Nasri, R., Lassoued, I., Souissi, N., Mbarek, A. Barkia. (2013). Chemical and biophysical properties of gelatins extracted from alkali-pretreated skin of cuttlefish (Sepia officinalis) using pepsin. Food Research International 55, 1680-1687
  13. Kaewruang, P., Benjakul,S., Prodpran, T, Nalinanon, S. (2013). Physicochemical and functional properties of gelatin from the skin of unicorn leatherjacket (Aluterus monoceros) as affected by extraction condition. Food Bioscience 2: 1-9
  14. Ktari.,N., Bkhairia,I., Jridi,M, Hamza.I, Riadh., B.S, Nasri, M. (2014). Digestive acid protease from Zebra blenny (Salaria basilisca) characteristics and application in gelatin extraction. Food Reseaarch International 57: 218-224
  15. Lassoued,I., Jridi.,M., Nasri,R., Dammak,A., Hajji, M, Nasri, M, Barkia,A (2014). Characteristics and Functional properties of gelatin from thornback ray skin obtained by pepsin aided process in comparison with commercial halal bovine gelatin. Food Hydrocolloids 41: 308 – 318
  16. Mulyani, S., Setyabudi,F.M.C.S, Pranoto, Y, Santoso, U. (2016). The Characteristic of buffalo hide as Raw material for gelatin production. Journal of Applied Food Technology, 3 (2)
  17. Mulyani, S., Setyabudi,F.M.C.S, Pranoto, Y, Santoso, U. (2017). The effect of pretreatment using hydrochloric acid on the characteristics of buffalo hide gelatin. Journal of the Indonesian Tropical Animal Agric.ulture 42, 14–22
  18. Mutilangi, W. A. M., Panyam, D., Kilara, A. (1995). Hydrolysates from proteolysis of heat-denatured whey proteins. Journal of Food Science, 60:1104–1109
  19. Ofori, R., (1999). Preparation of Gelatin from Fish Skin by an Enzyme Aided Process. Macdonald Campus of McGill University, Montreal, Cananda
  20. Sila.,A.,Alvarez O.M.,Haddar.,A. Gomez-Guille, M.C.,Nasri.,M.,.Montero.,M.P, Bougatef.,A. (2015). Recovery, viscoelastic and functional properties of barbel skin gelatine: investigation of anti-DPP-IV and anti-prolyl endopeptidase activities of generated gelatine polypeptides Food Chemistry 108: 478-486
  21. Surh, J., Decker, E.A., Clements, D.J. (2006). Properties and Stabiity of oil in water emulsions stabilized by fish gelatin. Food Hydrocolloids 20: 596-606
  22. Wu, T., Sun, L.-C., Du, C.-H., Cai, Q.-F., Zhang, Q.-B., Su, W.-J. (2009). Identification of pepsinogens and pepsins from the stomach of european eel (Anguilla anguilla). Food Chemistry, 115(1), 137–142

Last update: 2021-07-26 16:54:01

No citation recorded.

Last update: 2021-07-26 16:54:01

No citation recorded.