Karakteristik Kolagen dari Kulit dan Sisik Ikan Coklatan, Swanggi, dan Kurisi sebagai Bahan Gelatin Characteristics of Collagen Skin and Scales of Lattice Monocle Bream, Purple-Spotted Bigeye and Threadfin Bream as Gelatin Ingredients
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Accepted
29 December 2022
Published
30 December 2022
Keywords:
-
deproteinization, histology, hydroxyproline, SDS-PAGE
Abstract
The by-product of the fish fillet industry for lattice monocle bream, purple-spotted bigeye and threadfin bream, are only used as an ingredient for animal feed although it can be used as a source of collagen and gelatin. The hydroxyproline content forming collagen along with the properties of collagen protein is not yet available, so research is done. This study was aimed to determine the selected skin type as a gelatin material by taking into account the characteristics of the skin and scales of lattice monocle bream, purple-spotted bigeye, threadfin bream, and hydroxyproline content as a collagen marker. The experimental design used at the deproteination stage used a Randomized Block Design (RBD) with three factors where the first factor was the type of fish consisting of three levels (lattice monocle bream, purple-spotted bigeye and threadfin bream), the second factor was the soaking time of NaOH 12 levels (2; 4; 6; 8; 10; 12; 14; 16; 18; 20; 22; 24) hours, the third factor of the skin type is three levels (skin, scales, scaly skin), The experimental design in this study was analyzed by statistic with ANOVA and Duncan’s advanced test. The results showed that the deproteinization optimization time of NaOH immersion started from 14-20 hours depending on the type of fish and the raw materials, effectively eliminated non-collagen proteins. The area of collagen tissue in histology test preparations was ±95.136,16 µm² highest in the scaly skin of the purple-spotted bigeye associated with the highest protein content in purple-spotted bigeye scaly skin of 21.20±0.18% (wet basis) 56.17±0.12% (dry basis). The skin type had a molecular weight in the range of 10 to 105 kDa. The raw material contains protein which is sarcoplasmic protein, myofibrils and collagen containing connective tissue, so the raw material can be used as a gelatin producer. The scaly skin of purple spotted bream has the highest hydroxyproline than other skin types of 0.0888 µg/µL, so it can be determined as the selected skin types.
References
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Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., & Shahidi, F. (2010). Comparative study on characteristics of gelatin from the skins of brownbanded bamboo shark and blacktip shark as affected by extraction conditions. Food Hydrocolloids, 24(2–3), 164–171. doi:10.1016/j.foodhyd.2009.09.001
Kruger, N. J. (2002). The Protein Protocols Handbook Second Edition. (J. M. Walker, Ed.). Humana Press Inc.
Laemmli, U. K.. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685. doi:10.1038/227680a0
Meng, D., Tanaka, H., Kobayashi, T., Hatayama, H., Zhang, X., Ura, K., Yunoki, S., & Takagi, Y. (2019). The effect of alkaline pretreatment on the biochemical characteristics and fibril-forming abilities of types I and II collagen extracted from bester sturgeon by-products. International Journal of Biological Macromolecules, 131, 572–580. doi:10.1016/j.ijbiomac.2019.03.091
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Nirwandar, S. (2020). Halal Gelatin and its Business Opportunity in Indonesia. International Journal of Halal Research, 2(1), 50–57.
Nurdiani, R., Prihanto, A., Firdaus, M., & Kim. (2020). Seafood as source of protein‐based functional foods. Encyclopedia of Marine Biotechnology, 5(1), 2987-2997.
Nurilmala, M., Jacoeb, A. M., & Dzaky, R. A. (2017). Karakteristik gelatin kulit ikan tuna sirip kuning. Jurnal Pengolahan Hasil Perikanan Indonesia, 20(2), 339. doi:10.17844/jphpi.v20i2.18049
Nurilmala, M., Jacoeb, A. M., Sinaga, Y., Sudrajat, A. O., Budiardi, T., Wahju, R. I., & Kamal, M. M. (2022). Karakteristik protein dan struktur jaringan serta steroid ikan sidat (Anguilla bicolor bicolor) berdasarkan lokasi daging berbeda. Jurnal Pengolahan Hasil Perikanan Indonesia, 25(1), 97-106.
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Qin, D., You, X., Wang, M., Cong, X., Yuan, C., Yu, M., Cheng, X., & Chen, X. G. (2022). Development and application of fish scale wastes as versatile natural biomaterials. Chemical Engineering Journal, 428(2022). 131102. doi:10.1016/j.cej.2021.131102
Rabotyagova, O. S., Cebe, P., & Kaplan, D. L. (2008). Collagen structural hierarchy and susceptibility to degradation by ultraviolet radiation. Materials Science and Engineering C., 28(8), 1420–1429. doi:10.1016/j.msec.2008.03.012
Reátegui-Pinedo, N., Salirrosas, D., Sánchez-Tuesta, L., Quiñones, C., Jáuregui-Rosas, S. R., Barraza, G., Cabrera, A., Ayala-Jara, C., Martinez, R. M., Baby, A. R., & Prieto, Z. A. (2022). Characterization of collagen from three genetic lines (gray, red and F1) of Oreochromis niloticus (tilapia) skin in young and old adults. Molecules, 27(3), 1123.
Rosmawati, Abustam, E., Tawali, A. B., Said, M. I., & Sari, D. K. (2018). Effect of body weight on the chemical composition and collagen content of snakehead fish Channa striata skin. Fisheries Science, 84(6), 1081–1089. doi:10.1007/s12562-018-1248-8
Safithri, M., Tarman, K., Suptijah, P., & Widowati, N. (2019). Karakteristik fisikokimia kolagen larut asam dari kulit ikan parang-parang (Chirocentrus dorab). Jurnal Pengolahan Hasil Perikanan Indonesia, 22(3), 441–452.
Sheehan, D. C., & Hrapchak, B. B. (1980). Theory and practice of histotechnology. Journal of Clinical Pathology, 34(12),1406–1406. doi:10.1136/jcp.34.12.1406-c
Sigma-aldrich. (2021). Technical Bulletin. https://www.sigmaaldrich.com/ID/en
Silva, T. H., Moreira-Silva, J., Marques, A. L. P., Domingues, A., Bayon, Y., & Reis, R. L. (2014). Marine origin collagens and its potential applications. Marine Drugs, 12(12), 5881–5901. doi:10.3390/md12125881
Song, Z., Liu, H., Liwen, C. Leilei, C., Zhou, C., Hong, P., & Deng, C. (2021). Characterization and comparison of collagen extracted from the skin of the nile tilapia by fermentation and chemical pretreatment. Food Chemistry. 340, 128139. doi:10.1016/j.foodchem.2020.128139
Srinivasan, S., & Durairaj, B. (2021). Collagen isolation and characterization from Sardinella longiceps. Journal of Advanced Veterinary and Animal Research. 8(4), 679–686. doi:10.5455/javar.2021.h560
Suvik, A., & Effendy, A. W. M. (2012). The use of modified masson’s trichrome staining in collagen evaluation in wound healing study. Malaysian Journal of Veterinary Research, 3(1), 39–47.
Suwandi, R., Nurjanah, & Winem, M. (2014). Proporsi bagian tubuh dan kadar proksimat ikan gabus pada berbagai ukuran. Jurnal Pengolahan Hasil Perikanan Indonesia, 17, 22–28.
van der Rest, M., & Garrone, R. (1991). Collagen family of proteins. FASEB Journal: Official publication of the Federation of American Societies for Experimental Biology, 5(13), 2814–2823.
Wahyuni, Kumorowati, E., Pitriani, & Achmad, H. (2015). Pengembangan metode pewarnaan histologi khusus trichome masson’s untuk diagnosa penyakit pada hewan. Diagnosa Veteriner, 14(3).
Xu, S., Yang, H., Shen, L., & Li, G. (2017). Purity and yield of collagen extracted from southern catfish (Silurus meridionalis Chen) skin through improved pretreatment methods. International Journal of Food Properties. 20(1), S141–S153. doi:10.1080/10942912.2017.1291677
Andriani, D., & Masyitha, D. (2017). Struktur histologi kulit ikan gabus (Channa striata). Jimvet, 01(3), 283–290.
Arumugam, G. K. S., Sharma, D., Balakrishnan, R. M., & Ettiyappan, J. B. P. (2018). Extraction, optimization and characterization of collagen from sole fish skin. Sustainable Chemistry and Pharmacy, 9 March, 19–26. doi:10.1016/j.scp.2018.04.003.
Atma, Y. (2017). Amino acid and proximate composition of fish bone gelatin from different warm-water species: A comparative study. IOP Conf. Series: Earth and Environmental Science, 58. doi:10.1088/1755-1315/58/1/012008.
Bielajew, B. J., Hu, J. C., & Athanasiou, K. A. (2020). Collagen: quantification, biomechanics, and role of minor subtypes in cartilage. Nature Reviews Materials, 5(10), 730–747. doi:10.1038/s41578-020-0213-1
Boran, G., Lawless, H. T., & Regenstein, J. M. (2010). Effects of extraction conditions on the sensory and instrumental characteristics of fish gelatin gels. Journal of Food Science, 75(9). doi:10.1111/j.1750-3841.2010.01827.x.
Badan Pusat Statistik. (2022, Agustus 27). Impor gelatin. https://www.bps.go.id./
Badan Standardisasi Nasional. (1992). SNI (Standar Nasional Indonesia) 01-2891–19:1–36 tentang cara uji makanan dan minuman. Badan Standardisasi Nasional.
Chuaychan, S., Benjakul, S., & Nuthong, P. (2016). Element distribution and morphology of spotted golden goatfish fish scales as affected by demineralisation. Food Chemistry, 197, 814–820.
Ebadi, Z., Khodanazary, A., Hosseini, S. M., & Zanguee, N. (2019). The shelf life extension of refrigerated Nemipterus japonicus fillets by chitosan coating incorporated with propolis extract. International Journal of Biological Macromolecules, 139, 94–102. doi:10.1016/j.ijbiomac.2019.07.204
Elliott, D. G. (2011). The skin: Functional morphology of the integumentary system in fishes. Encyclopedia of Fish Physiology,1, 476-488.
Ferreira, A. M., Gentile, P., Chiono, V., & Ciardelli, G. (2012). Collagen for bone tissue regeneration. Acta biomaterialia, 8(9), 3191–3200. doi:10.1016/j.actbio.2012.06.014
Gandhi, K., Sharma, N., Gautam, P. B., Sharma, R., Mann, B., & Pandey, V. (2022). Polyacrylamide gel electrophoresis BT. Advanced Analytical Techniques in Dairy Chemistry. Springer.
Gelse K, Pöschl E, Aigner T. 2003. Collagens - Structure, function, and biosynthesis. Advanced Drug Delivery Reviews. 55(12):1531–1546. doi:10.1016/j.addr.2003.08.002.
Gomez-Guillen, M. C., Turnay, J., Fernandez-Diaz, M. D., Ulmo, N., Lizarbe, M. A., & Montero, P. (2002). Structure and physical of gelatin extracted from different marine species: A comparative study. Food Hydrocolloids, 16, 25–34.
Haryati, D., Nadhifa, L., Humairah, & Abdullah, N. (2019). Ekstraksi dan karakterisasi gelatin kulit ikan baronang (Siganus canaliculatus) dengan metode enzimatis menggunakan enzim bromelin. Canrea jornal, 2(1), 26–31.
He, Q., & Xiao, K. (2016). The effects of tangerine peel (Citri reticulatae pericarpium) essential oils as glazing layer on freshness preservation of bream (Megalobrama amblycephala) during superchilling storage. Food Control, 69, 339–345. doi:10.1016/j.foodcont.2016.05.019
Jafari, H., Lista, A., Siekapen, M. M., Ghaffari-Bohlouli, P., Nie, L., Alimoradi, H., & Shavandi, A. (2020). Fish collagen: Extraction, characterization, and applications for biomaterials engineering. Polymers, 12(10),1–37. doi:10.3390/polym12102230
Kartika, I. W. D., Trilaksani, W., & Adnyane, I. K. M. (2017). Characterization of collagen from swim bladder waste of yellow-pike (Muraenesox talabon) by acid and hydrothermal extraction. Jurnal Pengolahan Hasil Perikanan Indonesia, 19(3), 222. doi:10.17844/jphpi.v19i3.15074
Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T., & Tanaka, M. (2005). Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chemistry, 89(3), 363–372. doi:10.1016/j.foodchem.2004.02.042
Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., & Shahidi, F. (2010). Comparative study on characteristics of gelatin from the skins of brownbanded bamboo shark and blacktip shark as affected by extraction conditions. Food Hydrocolloids, 24(2–3), 164–171. doi:10.1016/j.foodhyd.2009.09.001
Kruger, N. J. (2002). The Protein Protocols Handbook Second Edition. (J. M. Walker, Ed.). Humana Press Inc.
Laemmli, U. K.. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685. doi:10.1038/227680a0
Meng, D., Tanaka, H., Kobayashi, T., Hatayama, H., Zhang, X., Ura, K., Yunoki, S., & Takagi, Y. (2019). The effect of alkaline pretreatment on the biochemical characteristics and fibril-forming abilities of types I and II collagen extracted from bester sturgeon by-products. International Journal of Biological Macromolecules, 131, 572–580. doi:10.1016/j.ijbiomac.2019.03.091
Mo, W., Man, Y., & Wong, M. (2017). Use of food waste, fish waste and food processing waste for China’s aquaculture industry. The Science of the total environment, 613-614, 635-643. 10.1016/j.scitotenv.2017.08.321
Mudalal, S., Babini, E., Cavani, C., & Petracci, M. (2014). Quantity and functionality of protein fractions in chicken breast fillets affected by white striping. Poultry Science, 93(8), 2108-2116.
Nirwandar, S. (2020). Halal Gelatin and its Business Opportunity in Indonesia. International Journal of Halal Research, 2(1), 50–57.
Nurdiani, R., Prihanto, A., Firdaus, M., & Kim. (2020). Seafood as source of protein‐based functional foods. Encyclopedia of Marine Biotechnology, 5(1), 2987-2997.
Nurilmala, M., Jacoeb, A. M., & Dzaky, R. A. (2017). Karakteristik gelatin kulit ikan tuna sirip kuning. Jurnal Pengolahan Hasil Perikanan Indonesia, 20(2), 339. doi:10.17844/jphpi.v20i2.18049
Nurilmala, M., Jacoeb, A. M., Sinaga, Y., Sudrajat, A. O., Budiardi, T., Wahju, R. I., & Kamal, M. M. (2022). Karakteristik protein dan struktur jaringan serta steroid ikan sidat (Anguilla bicolor bicolor) berdasarkan lokasi daging berbeda. Jurnal Pengolahan Hasil Perikanan Indonesia, 25(1), 97-106.
Ozsvar, J., Yang, C., Cain, S., Baldock, C., Tarakanova, A., & Weiss, A. (2021). Tropoelastin and elastin assembly. Frontiers in Bioengineering and Biotechnology, 9, 1-11.
Pusat Data Statistik dan Informasi Kementerian Kelautan dan Perikanan. (2022). Pengolahan Data Produksi Kelautan dan Perikanan. (2022, Oktober 07). https://statistik.kkp.go.id.
Qin, D., You, X., Wang, M., Cong, X., Yuan, C., Yu, M., Cheng, X., & Chen, X. G. (2022). Development and application of fish scale wastes as versatile natural biomaterials. Chemical Engineering Journal, 428(2022). 131102. doi:10.1016/j.cej.2021.131102
Rabotyagova, O. S., Cebe, P., & Kaplan, D. L. (2008). Collagen structural hierarchy and susceptibility to degradation by ultraviolet radiation. Materials Science and Engineering C., 28(8), 1420–1429. doi:10.1016/j.msec.2008.03.012
Reátegui-Pinedo, N., Salirrosas, D., Sánchez-Tuesta, L., Quiñones, C., Jáuregui-Rosas, S. R., Barraza, G., Cabrera, A., Ayala-Jara, C., Martinez, R. M., Baby, A. R., & Prieto, Z. A. (2022). Characterization of collagen from three genetic lines (gray, red and F1) of Oreochromis niloticus (tilapia) skin in young and old adults. Molecules, 27(3), 1123.
Rosmawati, Abustam, E., Tawali, A. B., Said, M. I., & Sari, D. K. (2018). Effect of body weight on the chemical composition and collagen content of snakehead fish Channa striata skin. Fisheries Science, 84(6), 1081–1089. doi:10.1007/s12562-018-1248-8
Safithri, M., Tarman, K., Suptijah, P., & Widowati, N. (2019). Karakteristik fisikokimia kolagen larut asam dari kulit ikan parang-parang (Chirocentrus dorab). Jurnal Pengolahan Hasil Perikanan Indonesia, 22(3), 441–452.
Sheehan, D. C., & Hrapchak, B. B. (1980). Theory and practice of histotechnology. Journal of Clinical Pathology, 34(12),1406–1406. doi:10.1136/jcp.34.12.1406-c
Sigma-aldrich. (2021). Technical Bulletin. https://www.sigmaaldrich.com/ID/en
Silva, T. H., Moreira-Silva, J., Marques, A. L. P., Domingues, A., Bayon, Y., & Reis, R. L. (2014). Marine origin collagens and its potential applications. Marine Drugs, 12(12), 5881–5901. doi:10.3390/md12125881
Song, Z., Liu, H., Liwen, C. Leilei, C., Zhou, C., Hong, P., & Deng, C. (2021). Characterization and comparison of collagen extracted from the skin of the nile tilapia by fermentation and chemical pretreatment. Food Chemistry. 340, 128139. doi:10.1016/j.foodchem.2020.128139
Srinivasan, S., & Durairaj, B. (2021). Collagen isolation and characterization from Sardinella longiceps. Journal of Advanced Veterinary and Animal Research. 8(4), 679–686. doi:10.5455/javar.2021.h560
Suvik, A., & Effendy, A. W. M. (2012). The use of modified masson’s trichrome staining in collagen evaluation in wound healing study. Malaysian Journal of Veterinary Research, 3(1), 39–47.
Suwandi, R., Nurjanah, & Winem, M. (2014). Proporsi bagian tubuh dan kadar proksimat ikan gabus pada berbagai ukuran. Jurnal Pengolahan Hasil Perikanan Indonesia, 17, 22–28.
van der Rest, M., & Garrone, R. (1991). Collagen family of proteins. FASEB Journal: Official publication of the Federation of American Societies for Experimental Biology, 5(13), 2814–2823.
Wahyuni, Kumorowati, E., Pitriani, & Achmad, H. (2015). Pengembangan metode pewarnaan histologi khusus trichome masson’s untuk diagnosa penyakit pada hewan. Diagnosa Veteriner, 14(3).
Xu, S., Yang, H., Shen, L., & Li, G. (2017). Purity and yield of collagen extracted from southern catfish (Silurus meridionalis Chen) skin through improved pretreatment methods. International Journal of Food Properties. 20(1), S141–S153. doi:10.1080/10942912.2017.1291677
Authors
WidiyantoW., UjuU., & NurilmalaM. (2022). Karakteristik Kolagen dari Kulit dan Sisik Ikan Coklatan, Swanggi, dan Kurisi sebagai Bahan Gelatin: Characteristics of Collagen Skin and Scales of Lattice Monocle Bream, Purple-Spotted Bigeye and Threadfin Bream as Gelatin Ingredients. Jurnal Pengolahan Hasil Perikanan Indonesia, 25(3), 512-527. https://doi.org/10.17844/jphpi.v25i3.43598
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