ISOLASI DAN KARAKTERISASI KOLAGEN DARI KULIT IKAN PATIN (Pangasius sp.)

Pipih Suptijah, Dini Indriani, Supriyono Eko Wardoyo

Abstract


Isolation and Characterization of Collagen from the Skin of Catfish (Pangasius sp.)

 

          Skin of catfish is one of aquatic by-products which could be used as an alternative source of collagen. This research is aimed to isolate and characterize collagen from skin of catfish. Methods of  isolation of collagen included three stages, the first was deproteinization using NaOH solution with concentration of 0.05 M; 0.10 M; 0.15 M; 0.20 M for 12 hours, the second was soaking in CH3COOH solution with concentration of 0.05 M; 0.10 M; 0.15 M; and 0.20 M for 2 hours, and the third was extraction in water at a temperature of 40 0C for 2 hours; characterization of collagen was included chemical and physical properties. The results showed that the best extraction method ofcollagen from skin of catfish was soaking the skin in 0.05 M NaOH solution for 12 hours and soaking the skin in 0.05 M acetic acid for 2 hours. Extraction yields of collagen was 12.15%. Chemical characteristics included proximate and amino acid composition. Proximate value of collagen consisted of moisture was 6.55%, ash 1.80%,  protein 64.74% and fat 8.85%.  The major amino acid composition of collagen were glycine, proline, alanine, arginine and glutamate. Physical characteristics of collagen resulted from FTIR analysis showed amide A, amide B, amide I, amide II and amide III, triple helical structure of the amide I and amide III indicates that the compound produced was collagen; color analysis was 66.39%; thermal analysis showed a melting temperature peak was 154.47 0C and pH value was 5.34.

Keywords : Catfish, isolation, characterization, collagen, skin

 

ABSTRAK

          Kulit ikan patin merupakan salah satu limbah hasil perairan yang dapat digunakan sebagai sumber alternatif kolagen. Penelitian ini bertujuan untuk mengisolasi dan karakterisasi kolagen yang diperoleh dari kulit ikan patin. Isolasi kolagen yang dilakukan meliputi tiga tahap, yaitu tahap pertama adalah proses deproteinisasi menggunakan larutan NaOH dengan konsentrasi, yaitu 0,05 M; 0,10 M; 0,15 M; 0,20 M dan lama waktu perendaman selama 12 jam; tahap kedua, yaitu perendaman dalam larutan CH3COOH dengan empat konsentrasi CH3COOH yaitu 0,05 M; 0,10 M; 0,15 M; dan 0,20 M dan lama waktu perendaman selama 2 jam; dan tahap ketiga, yaitu ekstraksi dengan air pada suhu 40 0C selama 2 jam; serta karakterisasi kolagen yang dilakukan, meliputi sifat kimia dan fisik. Hasil penelitian menunjukkan bahwa metode ekstraksi kolagen dari kulit ikan patin  terbaik diperoleh melalui proses perendaman kulit dalam larutan NaOH 0,05 M selama 12 jam dan  perendaman kulit dalam asam asetat 0,05 M selama 2 jam.  Rendemen serbuk kolagen yang dihasilkan sebesar 12,15 %. Karakteristik kimia meliputi proksimat dan komposisi asam amino. Nilai proksimat kolagen terdiri dari kadar air 6,55 %,  abu 1,80 %, protein 64,74 % dan lemak 8,85 %. Komposisi asam amino yang dominan pada kolagen adalah glisina, prolina, alanina, arginina dan glutamat. Karakteristik fisik kolagen yang dihasilkan adalah analisis FTIR menunjukkan adanya gugus amida A, amida B, amida I, amida II dan amida III, struktur triple heliks pada amida I dan amida III mengindikasikan bahwa senyawa yang dihasilkan adalah kolagen; analisis warna  yaitu 66,39 %; analisis termal yang menunjukkan suhu puncak pelelehan adalah 154,47 0C dan nilai pH kolagen yaitu 5,34.


 

Kata kunci : Ikan patin, isolasi, karakterisasi, kolagen, kulit 


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References


Ahmad, M., & Benjakul, S. (2010). Extraction and characterisation of pepsinsolubilised collagen from the skin of unicorn leatherjacket (Aluterus monocerous). Food Chem, 120, 817-824.

Association of Official Analytical Chemist. (1995). Official methods of analysis. Washington, DC: The Association of Official Analytical Chemist. Inc.

Association of Official Analytical Chemist. (2005). Official methods of analysis (18 Edn). Mayland. USA: Association of Official Analytical Chemist Inc.

Apriyantono, A., Fardiaz, D., Puspitasari, N.L., Yasni, S., & Budiyanto, S. (1989). Analisis pangan. Bogor: IPB Press.

.

Ariesta, C. (2014). Ekstraksi dan karakterisasi kolagen dari kulit ikan cobia (Rachycentron canadum) (skripsi). Bogor: Departemen Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu Kelautan, IPB.

Chai, H.J., Li, J.H., Huang, H.N., Li, T.L., Chan, Y.L., Shiau, C.Y., & Wu1, C.J. (2010). Effects of sizes and conformations of fish-scale collagen peptides on facial skin qualities and transdermal penetration efficiency. J Biomed Biotechnol, 2010, 1-9. doi:10.1155/2010/757301.

Coates, J. (2000). Interpretation of infrared spectra, a practical approach. Di dalam: Meyers RA, editor. Encyclopedia of Analytical Chemistry. Chichester: John Wiley & Sons Ltd.

Duan, R., Zhang, J., Li, J., Zhong, X., Konno, K., & Wen, H. (2012). The effect of the subunit composition on the thermostability of collagens from the scales of freshwater fish. Food Chem, 135, 127-132.

Friess, W. (1998). Collagen – biomaterial for drug delivery. Eur J Pharm Biopharm, 45, 113-136.

Gaurav, S. (2003). Digital color imaging handbook. CRC Press. ISBN 084930900X.

Gime´nez, B., Turnay, J., Lizarbe, M.A., Montero, P., & Go´mez-Guillen,M.C. (2005). Use of lactic acid for extraction of fish skin gelatin. Food Hydrocolloid, 19, 941-950

Gómez-Guillén, M.C., Turnay, J., Fernández-Dı́az, M.D., Ulmo, N., Lizarbe, M.A., & Montero, P. (2002). Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocolloid, 16, 25-34.

Haris, M.A. (2008). Pemanfaatan limbah tulang ikan nila (Oreochromis niloticus) sebagai gelatin dan pengaruh lama penyimpanan pada suhu ruang (skripsi). Bogor: Departemen Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu Kelautan, IPB.

Hartati I., & Kurniasari, L. (2010). Kajian produksi kolagen dari limbah sisik ikan secara ekstrasi enzimatis. Momentum, 6 (1), 33-35.

Jamilah, B., Hartina, M.U., Hashim, D.M., & Sazili, A.Q. (2013). Properties of collagen from barramundi (Lates calcarifer) skin. International Food Research Journal 20 (2), 835-842.

Jaswir, I., Monsur, H.A., & Salleh, H.M. (2011). Nano-structural analysis of fish collagen extracts for new process development. Afr J Biotechnol, 10 (81), 18847- 18854.

Karim, A.A., & Bhat, R. (2009). Fish gelatin: properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocolloid, 23, 563-576.

Komsa-Penkova, R., Koynova, R., Kostov, G., & Tenchov, B.G. (1996). Thermal stability of calf skin collagen type I in salt solutions. Biochimica et Biophysica Acta, 1297, 171-181.

Kong, J., & Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta bioch bioph sin, 39 (8), 549-559.

Lee, C.H., Singla, A., & Lee, Y. (2001). Biomedical applications of collagen. Int J Pharm, 221, 1-22.

Mahardika, S. (2013). Isolasi dan karakterisasi kolagen nanopartikel dari kulit ikan cucut bambu (Chiloscyllium punctatum) (skripsi). Bogor: Program Studi Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu kelautan, IPB.

Martianingsih, N., & Atmaja, L. (2009). Analisis sifat kimia, fisik, dan termal gelatin dari ekstraksi kulit Ikan pari (himantura gerrardi) melalui variasi jenis larutan asam. Prosiding KIMIA FMIPA – ITS.

Muyonga, J.H., Cole, C.G.B., & Duodu, K.G. (2004a). Characterisation of acids soluble collagen from skins of young and adulti Nile perch (Lates niloticus). Food Chemistry 85(1), 81-89.

Muyonga, J.H., Cole, C.G.B., & Duodu, K.G. (2004b). 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 Chem, 86, 325-332.

Nagarajan, M., Benjakul, S., Prodpran, T., Songtipya, P., & Kishimura, H. (2012). Characteristics and functional properties of gelatin from splendid squid (Loligo formosana) skin as affected by extraction temperatures. Food Hydrocolloids, 29, 389-397.

Nalinanon, S., Benjakul, S.,, Kishimura, H., & Osako, K. (2011). Type I collagen from the skin of ornate threadfin bream (Nemipterus hexodon): Characteristics and effect of pepsin hydrolysis. Food Chem, 125, 500-507.

Nur’aenah, N. (2013). Ekstraksi dan karakterisasi kolagen dan nanopartikel kolagen dari kulit ikan pari (Pastinachus solocirostris) sebagai bahan baku kosmetik (tesis). Bogor: Sekolah Pascasarjana, IPB.

Peng, Y., Glattauer, V., Werkmeister, J.A., & Ramshaw, J.A.M. (2004). Evaluation for collagen products for cosmetic application. J Cosmestic Sci, 55, 327-341.

Potaros, T., Raksakulthai, N., Runglerdkreangkrai, J., & Worawattanamateekul, W. (2009). Characteristics of collagen from nile tilapia (Oreochromis niloticus) skin isolated by two different methods. Kasetsart Journal, 43, 584-593.

See, S.F., Hong, P.K.L., Wan, A.W.M., & Babji, A.S. (2010). Physicochemical of gelatins extracted from skin of different freshwater fish species. International Food Reseacrh Journal, 17, 809-816.

Shon, J., Ji-Hyun, E., Hwang, S.J., & Jong-Bang, E. (2011). Effect of processing conditions on functional properties of collagen powder from Skate (Raja kenojei) skins. Food Sci Biotechnol, 20 (1), 99-106.

Sistem Informasi Diseminasi Data Statistik Kelautan dan Perikanan. (2013). KKP targetkan produksi patin 11 juta ton. Diperoleh dari www.antaranews.com.

Singh, P., Benjakul, S., Maqsood, S., & Kishimura, H. (2011). Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chem, 124, 97-105.

Standar Nasional Indonesia 01-2891-1992. (1992). Cara uji makanan dan minuman. Jakarta: Badan Standarisasi Nasional.

Standar Nasional Indonesia 01-4866.-1998. (1998). Cara uji cemaran arsen dalam makanan. Jakarta: Badan Standarisasi Nasional.

Standar Nasional Indonesia 01-2354.6-2006. (2006a). Cara uji kimia Bagian 6: Penentuan kadar logam berat merkuri (Hg) pada produk perikanan. Jakarta: Badan Standarisasi Nasional.

Standar Nasional Indonesia 01-2354.7-2006. (2006b). Cara uji kimia Bagian 7: Penentuan kadar logam berat timbal (Pb) pada produk perikanan. Jakarta: Badan Standarisasi Nasional.

Standar Nasional Indonesia 7387-2009. (2009). Batas maksimum cemaran logam berat dalam pangan. Jakarta: Badan Standarisasi Nasional.

Standar Nasional Indonesia 8076:2014. (2014). Kolagen Kasar dari Sisik Ikan – Syarat Mutu dan Pengolahan. Jakarta: Badan Standarisasi Nasional.

Songchotikunpan, P., Tattiyakul, J., & Supaphol, P. (2008). Extraction and electrospinning of gelatin from fish skin. Int J Biol Macromol, 42, 247-255.

Steel, R.G.D., & Torrie, J.H. (1993). Prinsip dan Prosedur Statistika, Suatu Pendekatan Biometrik. Sumantri B, penerjemah. Terjemahan dari : Principles and Procedures of Statistics. Jakarta: Gramedia Pustaka Utama.

Thitipramote, N., & Rawkdkuen,S. (2011). Histological structure and chemical composition of the farmed giant catfish’s skin. J of Microsc soc Thai, 4(2), 89-93.

Yoshimura, K., Terashima, M., Hozan, D., & Shirai, K. (2000). Preparation and dynamic viscoelasticity characterization of alkali-solubilized collagen from shark skin. J Agric Food Chem, 48, 685-690.

Zhou, P., & Regenstein, J.M. (2005). Effects of alkaline and acid pretreatments on alaska pollock skin gelatin extraction. J Food Sci, 70 (6), C392-C396.




DOI: https://doi.org/10.31938/jsn.v8i1.106

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