Fat Reduction in Improving the Quality of Chicken Feet Gelatine for Functional Food Application
Fat reduction has been performed on crude gelatin extracted from chicken feet (shank) through curing process using sodium hydroxide and acetic acid in various proportions. This study was conducted to evaluate the best fat reduction condition by the addition of acetic acid at concentrations of 0, 2.5 and 5% (v/v) with decantation time 0, 6 and 12 hours on crude gelatine from curing process at a ratio of 1% acetic acid; 1% acetic acid with 1% NaOH; 1% acetic acid and 3% NaOH and without curing (initial gelatine). The analysis was carried out to determine the composition of gelatin and their byproducts to total solids, total fat and fat binding capacity. The results showed that the variation in the ratio of the addition of acetic acid and decantation time affect the composition of fat and fat-binding ability. Based on fat binding capacity (FBC), treatment of chicken feet gelatin with curing of 1% acetic acid and 3% NaOH and continued by the addition of 5% (v/v) acetic acid with a 12-hour decantation time resulted in gelatin with the best FBC of 7.4 g/g, fat content 1.0248% and total solids 2.7575%.
DOI : http://dx.doi.org/10.15408/jkv.v0i0.3149
AOAC. 2000. Official methods of analysis (17th ed.). Washington, DC (USA): Association of Official Analytical Chemists.
Arnesen JA, A Gildberg. 2002. Preparation and characterisation of gelatin from the skin of harp seal (Phoca groendlandica). BioresourceTechnology. 82(2):191–194.
Asghar A, RL Henrickson. 1982. Chemical, biochemical and nutritional characteristics of collagen in food systems. Adv. Food Res. 28:231-372.
Badii F, KN Howell. 2006. Fish gelatin: structure, gelling properties and interaction with egg albumen proteins. Food Hydrocolloids. 20:630– 640.
Foegeding E, TC Lanier, HO Hultin. 1996. Characteristics of edible muscle tissue. In O. R. Fennema (Ed.), Food Chemistry. New York (USA): Marcel Dekker.
Gelatin Manufacturer’s Institute of America, Inc. (GMIA) revised 2006. Standard methods for the testing of edible gelatin. Gelatin Manufacturers Institute of America, Inc. GMIA. 2012. Gelatin handbook. In: America GMIA, editor.
Gómez-Guillén MC, P Montore. 2001. Extraction of gelatin from megrim (Lepidorhombus boscii) skins with several organic acids. Journal of Food Science. 66(2):213-216.
Gomez-Guillen MC, B Gimenez, ME Lopez-Caballero, MP Montero. 2011. Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocolloids. 25: 1813-1827.
Gudmundsson M, H Hafsteinsson. 1997. Gelatin from cod skins as affected by chemical treatments. Journal of Food Science. 62:37–39.
Gustavson K. 1956. The chemistry and reactivity of collagen. New York (USA): Academic Press.
Hamada Y, Y Nagashima, K Shiomi. 2001. Identification of fish collagen as a new allergen. Bioscience Biotechnology Biochemistry. 65 (2):285–291.
Haug IJ, KI Draget, O Smidsrod. 2004. Physical and rheological properties of fish gelatin compared to mammalian gelatin. Food Hyd. 18:203-213.
Jamilah B, KG Harvinder. 2002. Properties of gelatins from skins of fish-black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chemistry. 77:81–84.
Jellouli K, R Balti, A Bougatef, N Hmidet, A Barkia, M Nasri. 2011. Chemical composition and characteristics of skin gelatin from grey triggerfish (Balistes capriscus). LWT - Food Science and Technology. 44:1965-1970.
Jones NR. 1977. Uses of gelatin in edible products. In AG Ward & A Courts (Eds.), The science and technology of gelatins. New York (USA): Academic Press.
Karim AA, R Bhat. 2009. Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatin. Food Hydrocolloids. 23:563-576.
Kim CJ, KH Kim, BK Choe. 1988. Effect of pH, swelling temperature, swelling time and various acids on the yields and physicochemical properties of pigskin gelatin gel. Korean J. Anim. Sci. 30:301-306.
Lasekan A, AF. Bakar, D Hashim. 2013. Potential of chicken by-products as sources of useful biological resources. Waste Management. 33: 552-565.
Lassoued I, M Jridi, R Nasri, A Dammak, M Hajji, M Nasri, A Barkia. 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. 41:309-318.
Lawal OS. 2004. Functionality of African locust bean (Parkia biglobossa) protein isolate: effects of pH, ionic strength and various protein concentrations. Food Chemistry, 86:345-355.
Lin YK, DC Liu. 2006. Effects of pepsin digestion at different temperatures and times on properties of telopeptide-poor collagen from bird feet. Food Chemistry. 94:621–625.
Muyonga JH, CGB Cole, KG Duodu. 2004. Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chemistry. 86:325–332.
Ninan G, J Jose, Z Abubacker. 2011. Preparation and characterization of gelatin extracted from the skins of rohu (Labeo rohita) and common carp (Cyprinus carpio). J Food Proc Preserv. 35:143-162.
Ninan G, Z Abubacker, J Jose. 2009. Physico-chemical and texture properties of gelatins and water gel desserts prepared from the skin of freshwater carps. Fish Technology. 48(1):67-74.
Ockerman HW, CL Hansen. 1988. Glue and Gelatin. England (UK): Ellis Horwood Ltd.
Purnomo E. 1992. Penyamakan kulit kaki ayam. Yogyakarta (ID): Kanisius.
Rahman N, S Jamalulail. 2012. Extraction, physicochemical characterizations and sensory quality of chicken feet gelatin. Borneo Science. 30:1-13.
Sadowska M, I Kolodziejska, C Niecikowska. 2003. Isolation of collagen from the skins of Baltic cod (Gadus morhua). Food Chemistry. 81:257-262.
Sakaguchi M, H Hori, T Ebihara, S Irie, M Yanagida, S Inouye. 1999. Reactivity of the Immunoglobulin E in Bovine Gelatin-Sensitive Children to Gelatins from Various Animals. Immunology. 96 (7):286–290.
Sarbon MN, F Badii, NK Howell. 2013. Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin. Food Hydrocolloids. 30:143-51.
SNI 06-3735 (1995) Mutu dan Cara Uji Gelatin. Badan Standardisasi Nasional, Jakarta. p. 1–2.
Wang L, BR Yang, R Wang, X Du. 2008. Extraction of pepsin-soluble collagen from grass carp (Ctenopharyngodon idella) skin using an artificial neural network. Food Chem. 111:683-686.
Zeugolis DI, ST Khew, ES, Y Yew, AK Ekaputra, YW Tong, LL Yung, DW Hutmacher, C Sheppard, Michael. 2008. Electro-spinning of pure collagen nano-fibres–Just an expensive way to make gelatin?. Biomaterials.15:2293-2305.
Zhang N, C Huang, S Ou. 2011. In vitro binding capacities of three dietary fibers and their mixture for four toxic elements, cholesterol, and bile acid. Journal of Hazardous Materials 186:236–239.
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