Sazan (Carasobarbus luteus) pulundan kolajen izolasyonunun yanıt yüzey yöntemiyle ile optimizasyonu

Yıl 2024, , 140 - 150, 01.06.2024

Ümran Cansu

https://doi.org/10.22392/actaquatr.1322432

Öz

Balıkların mekanik işlenmesi sırasında ayrılan pullar kolajen ürünleri üretiminin yanı sıra birçok farklı şekilde kullanılabilmektedir. Yüksek saflıkta doğal kolajen elde etmek için, balık pullarının kolajen olmayan proteinlerden arındırılması ve demineralizasyonunu gerçekleştirmek gerekmektedir. Bu nedenle, bu çalışmanın amacı kolajen ürünlerinin üretimi için daha yüksek verim ve kalite için sazan balığı (C. luteus) pullarında kolajen izolasyonunu sağlamaktır. Pulların demineralizasyonu yanıt yüzeyi metodolojisi ile optimize edilmiştir. Deneysel olarak mineralin yaklaşık 89.92±1.10’i uzaklaştırılmış ve bu, model tarafından tahmin edilen değerle oldukça tutarlı olmuştur. Balık puluna uygulanan işlemler sonucunda protein oranı %23.12’den %86.16’ya kadar çıkarılmıştır. Tüm işlemlerin sonunda proteinin %20.54’ü ve hidroksiprolinin %3.56'sı kaybedilmiştir. Ancak balık pul örneklerinde Hyp konsantrasyonu 23.85’ten 56.13 85 mg/g pula, Hyp/pro oranı ise %4.49’dan %6.51’e yükselmiştir. Mineral maddenin etkili bir şekilde uzaklaştırılması, balık pulundaki Hyp miktarı ve Hyp/pro oranının artması, uygulanan işlemlerin sonucunda kolajen olmayan bileşenlerin etkili bir şekilde ayrılmasının ve kolajen izolasyonunun sağlandığını göstermektedir.

Anahtar Kelimeler

Balık pulu, kolajen izolasyonu, optimizasyon, hidroksiprolin

Optimization of Collagen Isolation from Carp (Carasobarbus luteus) Scales using Response Surface Methodology

Öz

The scale, which is separated during the mechanical processing of fish, can be used in the production of collagen products as well as in many other different ways. To obtain high-purity natural collagen, it is necessary to remove non-collagenous proteins and perform demineralization of fish scales. Therefore, the aim of this study is to achieve collagen isolation from common carp (Carasobarbus luteus) scales for the production of collagen products with higher efficiency and quality. The demineralization of the scales was optimized using response surface methodology. Experimentally, approximately 89.92±1.10% of the mineral was removed, which closely matched the value predicted by the model. The protein content of the fish scales was increased from 23.12% to 86.16% after the applied procedures. At the end of all the processes, 20.54% of the protein and 3.56% of hydroxyproline (Hyp) were lost. However, the Hyp concentration in the fish scale samples increased from 23.85 to 56.13 mg/g scale, and the Hyp/pro ratio increased from 4.49% to 6.51%. The effective removal of mineral matter, the increase in the amount of Hyp in fish scales, and the increase in the Hyp/pro ratio demonstrate that the applied procedures successfully separate non-collagenous components and achieve collagen isolation.

Anahtar Kelimeler

Fish scale, collagen isolation, optimization, hydroxyproline

Kaynakça

• Amirrah, I. N., Lokanathan, Y., Zulkiflee, I., Wee, M. M. R., Motta, A., & Fauzi, M. B. (2022). A comprehensive review on collagen type I development of biomaterials for tissue engineering: From biosynthesis to bioscaffold. Biomedicines, 10(9), 2307. https://doi.org/10.3390/biomedicines10092307
• Association of Official American Chemists International (AOAC). (2000). Official methods of analysis, 17th Ed., William, H. (ed) Washington, DC.
• Boran, G., & Regenstein, J. M. (2009). Optimization of gelatin extraction from silver carp skin. Journal of Food Science, 74(8), E432-E441. https://doi.org/10.1111/j.1750-3841.2009.01328.x
• Cansu, Ü., & Boran, G. (2015). Optimization of a multi-step procedure for isolation of chicken bone collagen. Korean Journal for Food Science of Animal Resources, 35(4), 431. https://doi.org/10.5851/kosfa.2015.35.4.431
• Cansu, Ü., & Boran, G. (2022). Kinetic evaluation of gelatin extraction from chicken skin and the effect of some extraction parameters. Journal of Food Process Engineering, 45(4), e13995. https://doi.org/10.1111/jfpe.13995 Duan, R., Ying, L., & Zhang, Y. (2004). Monitoring the decalcifying process of fish scale by titration. Journal of Huaihai Institute of Technology (Natural Sciences Edition), 13, 54-6.
• Feng, X., Wenxue, Z., Yuanyuan, Q., & Huaibin, K. (2015). Optimization of demineralization on Cyprinus carpio haematopterus scale by response surface methodology. Journal of Food Science and Technology, 52, 1684-1690. https://doi.org/10.1007/s13197-013-1164-y
• Fengxiang, Z., Anning, W., Zhihua, L., Shengwen, H., & Lijun, S. (2011). Preparation and characterisation of collagen from freshwater fish scales. Food and Nutrition Sciences, 2(8), 818-823. https://doi.org/10.4236/fns.2011.28112
• Fratzl, P. (2008). Collagen: structure and mechanics, an introduction. In Collagen: structure and mechanics (pp. 1-13). Boston, MA: Springer US. https://doi.org/10.1007/978-0-387-73906-9
• Gornall, A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry, 177(2), 751-766. https://doi.org/10.1016/S0021-9258(18)57021-6
• Jaziri, A. A., Shapawi, R., Mokhtar, R. A. M., Noordin, W. N. M., & Huda, N. (2022). Biochemical and microstructural properties of lizardfish (Saurida tumbil) scale collagen extracted with various organic acids. Gels, 8(5), 266. https://doi.org/10.3390/gels8050266
• 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. https://doi.org/10.1016/j.foodchem.2004.02.042
• Pati, F., Adhikari, B., & Dhara, S. (2010). Isolation and characterization of fish scale collagen of higher thermal stability. Bioresource Technology, 101(10), 3737-3742. https://doi.org/10.1016/j.biortech.2009.12.133
• Sankar, S., Sekar, S., Mohan, R., Rani, S., Sundaraseelan, J., & Sastry, T. P. (2008). Preparation and partial characterization of collagen sheet from fish (Lates calcarifer) scales. International Journal of Biological Macromolecules, 42(1), 6-9. https://doi.org/10.1016/j.ijbiomac.2007.08.003
• Skierka, E., Sadowska, M., & Karwowska, A. (2007). Optimization of condition for demineralization Baltic cod (Gadus morhua) backbone. Food Chemistry, 105(1), 215-218. https://doi.org/10.1016/j.foodchem.2007.04.001
• Tümerkan, E. T. A., Cansu, Ü., Boran, G., Mac Regenstein, J., & Özoğul, F. (2019). Physiochemical and functional properties of gelatin obtained from tuna, frog and chicken skins. Food Chemistry, 287, 273-279. https://doi.org/10.1016/j.foodchem.2019.02.088
• Wang, Y., & Regenstein, J. M. (2009). Effect of EDTA, HCl, and citric acid on Ca salt removal from Asian (silver) carp scales prior to gelatin extraction. Journal of Food Science, 74(6), C426-C431. https://doi.org/10.1111/j.1750-3841.2009.01202.x
• Woessner Jr, J. F. (1961). The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid. Archives of Biochemistry and Biophysics, 93(2), 440-447. https://doi.org/10.1016/0003-9861(61)90291-0
• Yang, H., Wang, H., Huang, M., Cao, G., Tao, F., Shen, Q., ... & Yang, H. (2022). Repurposing fish waste into gelatin as a potential alternative for mammalian sources: A review. Comprehensive Reviews in Food Science and Food Safety, 21(2), 942-963. https://doi.org/10.1111/1541-4337.12920
• Zhang, X., Xu, S., Shen, L., & Li, G. (2020). Factors affecting thermal stability of collagen from the aspects of extraction, processing and modification. Journal of Leather Science and Engineering, 2, 1-29. https://doi.org/10.1186/s42825-020-00033-0