Main Article Content

Abstract

Gelatin has been widely used as an additive in food industry pharmaceutical, and  cosmetic. The similar physical appearance between bovine and porcine gelatin causes an issue for some communities like a Muslim due to awareness of halal food. This study aims to produce gelatin from femur bones of bovines with acid hydrolysis and their characteristics compared to standard gelatin of bovine and porcine. Bovine and porcine bones were soaked in 5% HCl for 10 days and every 2 days a HCl solution was replaced to get ossein. Ossein is hydrolyzed by gradual heating at 65, 75, and 85oC. Gelatin  confirmed by  the physico-chemical characters, FT-IR and analysis amino acid with HPLC.The results showed that the yield of bovine gelatin was 4.33%. The physico-chemical characters of bovine gelatin resulting from isolation and bovine gelatin standards are in conformity with porcine gelatin standards and meet the requirements of SNI 06-3735-1995 and GMIA. Therefore, bovine gelatin is specifically capable of substituting porcine gelatin for application in the pharmaceutical field. The FTIR spectrum of bovine gelatin shows the presence of amide A, amide I, amide II and amide III groups. The amino acid characters of gelatin were identified as glycine (13.57%) and proline (1.62%) for bovine gelatin and glycine (0.51%) and proline (0.09%) for porcine gelatin.

Keywords

Gelatine Femur bones of bovine Functional group Amino acid

Article Details

How to Cite
Sugita, P., Rifai, M., Ambarsari, L., Rahayu, D. U. C., & Dianhar, H. (2021). Gelatin Extraction and Characterization from Femur Bones of Bovine and Porcine with Acid Process. Jurnal Jamu Indonesia, 6(1), 32-41. Retrieved from http://jamu.journal.ipb.ac.id/index.php/JJI/article/view/188

References

  1. [GMIA]. 2012. Gelatin Handbook. Gelatin Manufactures Institute of America.
  2. Aisyah NNM, Nurul H, Azhar ME and Fazilah A. 2014, 'Poultry as an Alternative of GelatinSource'. Health and the Environment Journal, 5(1): 37-49 37.
  3. Al-Saidi GS, Al-Alawi A, Rahman MS, Guizani N. 2012. Fourier transform infrared (FTIR) spectroscopic study of extracted gelatin from shaari (Lithirinus microdon) skin: effects of extraction conditions.Internatioal Food Research Journal. 19(3): 1167–1173.
  4. Amqizal A.H.I., Al-Kahtani H.A., Ismail E.A., Hayat K., Jaswir I., 2017. Identification and verification of porcine DNA in commercial gelatin and gelatin containing processed foods. Food Control 78, 297–303.
  5. AOAC. 2005. Official methods of analysis of the Association of Official Analytical Chemists International, 18th ed. In Association of Official Analytical Chemists, Washington (D.C.)
  6. Badan Pusat Statistik (BPS). 2007, Statistik Perdagangan Luar Negeri Impor, Badan Pusat Statistik, Jakarta
  7. Cebi, N., Durak, M. Z., Toker, O. S., Sagdic, O., Arici, M. 2016. An evaluation of Fourier transforms infrared spectroscopy method for the classification and discrimination of bovine, porcine and fish gelatins. Food Chem, 190:1109–1115.
  8. Faried SM, Pemanfaatan Limbah Tulang Sapi Sebagai Adsorben Untuk Menyerap Logam Kadmium (Cd) dengan Menggunakan Aktivasi Na2CO3. [Laporan Tugas Akhir]. UII Yogjakarta, 2016
  9. Gómez-Guillén M.C., B. Giménez, M.E. López-Caballero, M.P. Montero. 2011. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25: 1813-1827
  10. Gómez-Guillén MC, Pérez-Mateos M, Gómez-Estaca J, López-Caballero E, Giménez B, & Montero P. 2009. Fish gelatin: a renewable material for developing active biodegradable films. Trends in Food Science & Technology, 20(1): 3-16
  11. Hafidz RMRN, Yaakob CM, Amin I, & Noorfaizan A. 2011. Chemical and functional properties of bovine and porcine skin gelatin. International Food Research Journal, 18: 813-817
  12. Hasan. 2007. Studi ekstraksi dari pembuatan gelatin tipe B dari kulit sapi. [skripsi]. Bogor (ID): Institut Pertanian Bogor.
  13. Hashim, D. M., Man, Y. B. C., Norakasha, R., Shuhaimi, M., Salmah, Y. Syahariza, Z. A. 2010. Potential use of Fourier transform infrared spectroscopy for differentiation of bovine and porcine gelatins. Food Chem, 118, 856–860.
  14. Hwang, J-H., Mizuta, S., Yokoyama, Y. andYoshinaka R. 2007. Purification and Characterization of Molecular Species of Collagen in the Skin of Skate (Raja kenojei). Food Chem, 100: 921-925
  15. Ikoma, T., Kobayashi, H., Tanaka, J., Walsh, D. and Mann, S. 2003. Physical Properties of Type I Collagen Extracted from Fish scales of Pagrus major and Oreochromisniloticus. Int J BiolMacromol, 32: 199-204.
  16. Jamaludin MK, Zaki NM, Ramli MA, Hashim DM, Ab Rahman S. 2011. Istihalah: Analysis on the utilization of gelatin in food products.
  17. Jannah dan Fatimah. 2008. Efektifitas Penggunaan Asam Sitrat dalam Pembuatan Gelatin Ikan Bandeng (Chanos chanos Forskal). [Skripsi]. Jurusan Kimia, Fakultas Sains dan Teknologi, Universitas Islam Negeri Maulana Malik Ibrahim. Malang.
  18. Johns. P. dan A. Courts. 1977. Relation Between Collagen and gelatin. dalam: Ward. A.G. dan A. Courts (ed.). 1977. The Science and Technology of Gelatin. Acedemic Press. London.
  19. Jongjareonrak, A., Benjakul, S., Visessanguan, W., Prodpran, T. and Tanaka, M. 2006. Characterization of Edible Films from Skin Gelatin of Brownstripe Red Snapper and Bigeye Snapper. Food Hydrocolloids, 20: 492-501.
  20. Karlina IR, Atmaja L. 2010. Ekstraksi gelatin dari tulang rawan ikan pari (Himantura gerrardi) pada variasi larutan asam untuk perendaman [skripsi]. Surabaya (ID): Institut Tekhnologi Sepulun November.
  21. Kusumawati R, Tazwir, Wawasto A. 2008. Pengaruh perendaman dalam asam klorida terhadap kualitas gelatin ikan kakap merah (Lutjanus sp.). Jurnal Pascapanen dan Bioteknologi Perikanan dan Kelautan. 1(3): 63–68.
  22. Mariod A.A, Adam H. F. 2013, 'Review: Gelatin, Source, Extraction and Industrial, Applications', Acta Sci. Pol. Technol. Aliment. 12(2): 135-147.
  23. Masirah. 2018. Perbandingan karakteristik sifat fisikokimia gelatin tulang ikan bandeng dan gelatin sapi komersial. Prosiding Seminar Nasional Kelautan dan Perikanan IV: 285-292
  24. Pradini D., H. Juwono, K. A. Madurani, F. Kurniawan. 2018. A preliminary study of identification halal gelatin using quartz crystal microbalance (QCM) sensor. Malaysian Journal of Fundamental and Applied Sciences. 14(3): 325-330
  25. Puspawati MN, Simpen IN, Miwada INS. 2012. Isolasi gelatin dari kulit kaki ayam broiler dan analisis gugus fungsinya menggunakan spektrofotometri FTIR. J Chem. 6(1): 79–87.
  26. Rehman W. Ul, A. Majeed, R. Mehra, S. Bhushan, P. Rani, K. C. Saini and F. Bast. Gelatin: A comprehensive report covering its indispensable aspects. In: Natural Polymers: Derivatives, Blends and Composites Vol. I ISBN: 978-1 -63485-831-1 Editors: Saiqa Ikram and Shakeel Ahmed © 2016 Nova Science Publishers, Inc.
  27. Rusli A. 2004. Kajian Proses Ekstraksi Gelatin dari Kulit Ikan Patin (Pangasius hypopthalmus) Segar [Tesis]. Bogor: Sekolah Pasca Sarjana. IPB.
  28. Russell JD, Dolphin JM, Koppang MD. 2007. Selective analysis of secondary amino acids in gelatinusing pulsed electrochemical detection. Analytical Chemistry. 79: 6615-6621.
  29. Said, M.I., S Triatmojo., Y Erwanto., A. Fudholi. (2011). Karakteristik gelatin kulit kambing yang diproduksi melalui proses asam basa. J. Agritech. 31(3).
  30. Saputra, R.H., I. Widistuti & A.Supriadi. 2015. Karakteristik fisik dan kimia gelatin kulit ikan patin (Pangasius pangasius) dengan kombinasi berbagai asam dan suhu. Jurnal Teknologi Hasil Perikanan. 4 (1): 29-36.
  31. See, S. F., Hong, P. K., Ng, K. L., Wan Aida, W. M. and Babji, A. S. 2010, 'Physicochemical properties of gelatins extracted from skins of different freshwater fish species’, International Food Research Journal 17: 809-816 .
  32. Shyni K., G.S. Hema, G. Ninan, S. Mathew, C.G. Joshy, P.T. Lakshmanan 2014, 'Isolation and characterization of gelatin from the skins of skipjack tuna (Katsuwonus pelamis), dog shark (Scoliodon sorrakowah), and rohu (Labeo rohita)’. Food Hydrocolloids 39: 68-76.
  33. SNI 06-3735-1995. Mutu dan Cara Uji Gelatin. Badan Standardisasi Nasional, Jakarta. p. 1–2.
  34. Sopian I. 2002. Analisis sifat fisik, kimia, dan fungsional gelatin yang diekstrak dari kulit dan tulang ikan pari [Skripsi]. Bogor (ID): Institut Pertanian Bogor.
  35. Tong Y. and Tiejin Y. 2013. Gelling Strenght Improvement and Characterization of a Gelatin from Scales of Bighead Carp (Aristichthysnobilis). Jurnal of Food, Agriculture and Environment, 2(1), 146-150.
  36. Widyaninggar A, Triwahyudi, Triyana K, Rohman A. 2008. Differentiation between porcine and bovine gelatin in commercial capsule shells based on amino acid profiles and principal component analysis. J Pharm Indonesia. 23(2): 96–101.
  37. Yudiono H. 2003. Karakteristik fisikokimia gelatin hasil perendaman tulang sapi dalam campuran Ca(OH)2-CaCl2 [Skripsi]. Bogor (ID): Institut Pertanian Bogor.
  38. Yuiarifin H, Bintoro VP, Suwarasturi A. 2006. Pengaruh berbagai konsentrasi asam fosfat pada proses perendaman tulang sapi terhadap rendemen kadar abu dan viskositas gelatin. J Indon Trop Anim Agric. 31(1): 55–61.
  39. Zilhadia, Betha OS, Bayyinah. 2012. Analisis komposisi asam amino gelatin sapi dan gelatin babi pada produk kapsul lunak simulasi menggunakan teknik kombinasi high performance liquid chromatography (HPLC) dan principal component anaysis (PCA).[Slripsi]. Universitas Islam Negeri Hidayatullah.