Yield and Properties of Collagen from Nile Tilapia (Oreochromis niloticus) Scales: Effects of Ultrasonic Pretreatment on Pepsin-Aided Extraction
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Abstract
The yield and characteristics of collagen from Nile tilapia scale pretreated with ultrasound at 40 kHz for 2 h before pepsin-aided extraction for 12-72 h (US collagen) were investigated compared to collagen from the scales without ultrasonic pretreatment (non-US collagen). Both collagens' yields increased with prolonged extraction time (P<0.05). Nevertheless, the yield of ultrasound-pretreated collagen (2.20-4.31%) was approximately 2 times greater than that of collagen without ultrasonic pretreatment (1.06-2.03%) (P<0.05). The amino acid compositions of both collagens were comparable, consisting mainly of glycine, alanine, proline, and hydroxyproline (329-330, 115,119, 114-116, 85 residues per 1000 residues, respectively), and both were classified as type I collagen. Moreover, the thermal transition temperatures (39.38-39.43°C) and enthalpy (0.55 J/g) were comparable between both collagens (P>0.05). Analysis of the FTIR spectra indicated that the ultrasonication pretreatment of the scale before the collagen did not alter the triple-helical structure of the collagen. Therefore, pretreatment of the Nile tilapia scales with ultrasonication before the pepsin-aided process could increase yield without significantly affecting the characteristics and triple-helical structure of the collagen.
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References
Abe, Y., & Krimm, S. (1972). Normal vibrations of crystalline polyglycine I. Biopolymers, 11(9), 1817-1839. https://doi.org/10.1002/bip.1972.360110905
Ali, A. M. M., Benjakul, S., & Kishimura, H. (2017). Molecular characteristics of acid and pepsin soluble collagens from the scales of golden carp (Probarbus jullieni). Emirates Journal of Food and Agriculture, 29(6), 450-457. https://doi.org/10.9755/ejfa.2016-09-1316
Ali, A. M. M., Kishimura, H., & Benjakul, S. (2018). Extraction efficiency and characteristics of acid and pepsin soluble collagens from the skin of golden carp (Probarbus Jullieni) as affected by ultrasonication. Process Biochemistry, 66, 237-244. https://doi.org/10.1016/j.procbio.2018.01.003
AOAC. (2023). Official methods of analysis (22nd ed.). AOAC International.
Baite, T. N., Mandal, B., & Purkait, M. K. (2021). Ultrasound assisted extraction of gallic acid from Ficus auriculata leaves using green solvent. Food and Bioproducts Processing, 128, 1-11. https://doi.org/https://doi.org/10.1016/j.fbp.2021.04.008
Bavisetty, S. C. B., Karnjanapratum, S., Dave, J., Purba, D. T., Kudre, T., Maser, W. H., Maiyah, N., Kingwascharapong, P., & Ali, A. M. M. (2024). Ultrasonication on collagen yield, physiochemical and structural properties from seabass (Lates Calcarifer) scales as affected by pretreatment and extraction conditions. Natural and Life Sciences Communications, 23(1), Article e2024003. https://doi.org/10.12982/NLSC.2024.003
Bergman, I., & Loxley, R. (1963). Two improved and simplified methods for the spectrophotometric determination of hydroxyproline. Analytical Chemistry, 35(12), 1961-1965. https://doi.org/10.1021/ac60205a053
Boon-Ek, P. (2025, February 5). Monitoring Report: Nile tilapia and products (Febuary, 2024). Fisheries Economics Division, Department of Fisheries, Thailand. https://www.fisheries.go.th/strategy/fisheconomic/Monthly%20report/tilapia/2%20Tilapia%20กพ%202567.pdf
Chen, L., Cheng, G., Meng, S., & Ding, Y. (2022). Collagen membrane derived from fish scales for application in bone tissue engineering. Polymers, 14(13), Article 2532. https://doi.org/10.3390/polym14132532
Chen, S., Chen, H., Xie, Q., Hong, B., Chen, J., Hua, F., Bai, K., He, J., Yi, R., & Wu, H. (2016). Rapid isolation of high purity pepsin-soluble type I collagen from scales of red drum fish (Sciaenops ocellatus). Food Hydrocolloids, 52, 468-477. https://doi.org/10.1016/j.foodhyd.2015.07.027
Chinh, N. T., Manh, V. Q., Trung, V. Q., Lam, T. D., Huynh, M. D., Tung, N. Q., Trinh, N. D., & Hoang, T. (2019). Characterization of collagen derived from tropical freshwater carp fish scale wastes and its amino acid sequence. Natural Product Communications, 14(7), Article 1934578X19866288. https://doi.org/10.1177/1934578X19866288
Chuaychan, S., Benjakul, S., & Kishimura, H. (2015). Characteristics of acid- and pepsin-soluble collagens from scale of seabass (Lates calcarifer). LWT - Food Science and Technology, 63(1), 71-76. https://doi.org/10.1016/j.lwt.2015.03.002
Doyle, B. B., Bendit, E. G., & Blout, E. R. (1975). Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers, 14(5), 937-957. https://doi.org/10.1002/bip.1975.360140505
Duan, R., Zhang, J., Du, X., Yao, X., & Konno, K. (2009). Properties of collagen from skin, scale and bone of carp (Cyprinus carpio). Food Chemistry, 112(3), 702-706. https://doi.org/10.1016/j.foodchem.2008.06.020
Feng, H., Li, X., Deng, X., Li, X., Guo, J., Ma, K., & Jiang, B. (2020). The lamellar structure and biomimetic properties of a fish scale matrix. RSC Advances, 10(2), 875-885. https://doi.org/10.1039/c9ra08189e
Fujii, K. K., Taga, Y., Takagi, Y. K., Masuda, R., Hattori, S., & Koide, T. (2022). The thermal stability of the collagen triple helix Is tuned according to the environmental temperature. International Journal of Molecular Sciences, 23(4), Article 2040. https://doi.org/10.3390/ijms23042040
Huang, C.-Y., Kuo, J.-M., Wu, S.-J., & Tsai, H.-T. (2016). Isolation and characterization of fish scale collagen from tilapia (Oreochromis sp.) by a novel extrusion–hydro-extraction process. Food Chemistry, 190, 997-1006. https://doi.org/10.1016/j.foodchem.2015.06.066
Kim, H. K., Kim, Y. H., Kim, Y. J., Park, H. J., & Lee, N. H. (2012). Effects of ultrasonic treatment on collagen extraction from skins of the sea bass Lateolabrax japonicus. Fisheries Science, 78(2), 485-490. https://doi.org/10.1007/s12562-012-0472-x
Kittiphattanabawon, P., Sriket, C., Kishimura, H., & Benjakul, S. (2019). Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis nioticus) scale. Emirates Journal of Food and Agriculture, 31(2), 95-101. https://doi.org/10.9755/ejfa.2019.v31.i2.1911
Krimm, S., & Bandekar, J. (1986). Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Advances in Protein Chemistry, 38, 181-364. https://doi.org/10.1016/S0065-3233(08)60528-8
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685. https://doi.org/10.1038/227680a0
Li, L.-Y., Zhao, Y.-Q., He, Y., Chi, C.-F., & Wang, B. (2018). Physicochemical and antioxidant properties of acid-and pepsin-soluble collagens from the scales of Miiuy croaker (Miichthys miiuy). Marine Drugs, 16(10), Article 394. https://doi.org/10.3390/md16100394
Li, Z.-R., Wang, B., Chi, C.-F., Zhang, Q.-H., Gong, Y.-D., Tang, J.-J., Luo, H.-Y., & Ding, G.-F. (2013). Isolation and characterization of acid soluble collagens and pepsin soluble collagens from the skin and bone of Spanish mackerel (Scomberomorous niphonius). Food Hydrocolloids, 31(1), 103-113. https://doi.org/10.1016/j.foodhyd.2012.10.001
Liu, D., Liang, L., Regenstein, J. M., & Zhou, P. (2012). Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis). Food Chemistry, 133(4), 1441-1448. https://doi.org/10.1016/j.foodchem.2012.02.032
Liu, D., Zhang, X., Li, T., Yang, H., Zhang, H., Regenstein, J. M., & Zhou, P. (2015). Extraction and characterization of acid- and pepsin-soluble collagens from the scales, skins and swim-bladders of grass carp (Ctenopharyngodon idella). Food Bioscience, 9, 68-74. https://doi.org/https://doi.org/10.1016/j.fbio.2014.12.004
Mondal, J., Lakkaraju, R., Ghosh, P., & Ashokkumar, M. (2021). Acoustic cavitation-induced shear: a mini-review. Biophysical Reviews, 13(6), 1229-1243. https://doi.org/10.1007/s12551-021-00896-5
Moniruzzaman, S. M., Takahashi, K., Nesa, N. U., Keratimanoch, S., Okazaki, E., & Osako, K. (2019). Characterization of acid- and pepsin-soluble collagens extracted from scales of carp and lizardfish caught in japan, bangladesh and vietnam with a focus on thermostability. Food Science and Technology Research, 25(2), 331-340. https://doi.org/10.3136/fstr.25.331
Muyonga, J. H., Cole, C. G. B., & Duodu, K. G. (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(3), 325-332. https://doi.org/10.1016/j.foodchem.2003.09.038
Nalinanon, S., Benjakul, S., Visessanguan, W., & Kishimura, H. (2008). Tuna pepsin: characteristics and its use for collagen extraction from the skin of threadfin bream (Nemipterus spp.). Journal of Food Science, 73(5), C413-C419. https://doi.org/10.1111/j.1750-3841.2008.00777.x
Payne, K. J., & Veis, A. (1988). Fourier transform IR spectroscopy of collagen and gelatin solutions: Deconvolution of the amide I band for conformational studies. Biopolymers, 27(11), 1749-1760. https://doi.org/10.1002/bip.360271105
Plepis, A. M. D. G., Goissis, G., & Das-Gupta, D. K. (1996). Dielectric and pyroelectric characterization of anionic and native collagen. Polymer Engineering and Science, 36(24), 2932-2938. https://doi.org/10.1002/pen.10694
Shaik, M. I., Chong, J. Y., & Sarbon, N. M. (2021). Effect of ultrasound-assisted extraction on the extractability and physicochemical properties of acid and pepsin soluble collagen derived from Sharpnose stingray (Dasyatis zugei) skin. Biocatalysis and Agricultural Biotechnology, 38, Article 102218. https://doi.org/10.1016/j.bcab.2021.102218
Shalaby, M., Agwa, M., Saeed, H., Khedr, S. M., Morsy, O., & El-Demellawy, M. A. (2020). Fish scale collagen preparation, characterization and its application in wound healing. Journal of Polymers and the Environment, 28(1), 166-178. https://doi.org/10.1007/s10924-019-01594-w
Steel, R. G. D., & Torrie, J. H. (1980). Principles and procedures of statistics: A biometrical approach (2nd ed.). McGraw-Hill.
Tu, Z. C., Huang, T., Wang, H., Sha, X. M., Shi, Y., Huang, X. Q., Man, Z. Z., & Li, D. J. (2015). Physico-chemical properties of gelatin from bighead carp (Hypophthalmichthys nobilis) scales by ultrasound-assisted extraction. Journal of Food Science and Technology, 52(4), 2166-2174. https://doi.org/10.1007/s13197-013-1239-9
