Isolation and Characterization of Acid-Soluble Collagens from the Bone and Fins of the Barracuda (Sphyraena spp.) as Marine Collagen Sources

Noraishah Illiana Ibrahim, Siti Nur Hazwani Oslan, Rossita Shapawi, Ruzaidi Azli Mohd Mokhtar, Wan Norhana Md. Noordin, Rahmi Nurdiani, Nurul Huda

Abstract


Barracuda fish (Sphyraena sp.) bone and fins could be a source of aquatic collagen. Marine collagen has recently gained popularity due to its lack of infectious infections. This collagen extraction yields 1.99 % acetic acid-soluble collagen (AAC), 2.36 % lactic acid-soluble collagen (LAC), and 3.26 % citric acid-soluble collagen (CAC). AAC has a high L* value compared to LAC and CAC, indicating great brightness in color. For hydroxyproline content, the amount of collagen was 82.70, 81.31, and 80.93 for AAC, LAC, and CAC. AAC and LAC have maximum collagen solubility at pH 3, and CAC at pH 5. The effects of collagen solubility on NaCl concentrations drop substantially at 30 g/L for all collagen samples. All extracted collagen structures are type I collagen consisting of two chains (α1 and α2) based on SDS-PAGE analysis and possessing a complete triple helical structure based on UV absorption (229.5 nm) and Fourier Transformation Infrared Spectrometry (ATR-FTIR) showed all collagen samples had amide A, B, amide I, II, and III peaks. All collagens demonstrate strong heat resistance and structural stability as Tmax is above 30°C. LAC demonstrated higher absorption of water (0.50 0.01±mL/mg) and oil (0.70±0.07 mL/mg) than AAC and CAC. At pH 7, CAC and AAC reduced foam and foam case capacity. In emulsion properties, only AAC does not demonstrate important emulsion stability. AAC showed superior collagen than LAC and CAC based on physicochemical and functional qualities. Therefore, all collagen samples can be employed as replacements for terrestrial collagen in diverse applications.

Keywords


Barracuda fish (Sphyraena sp.); bone and fins; acid-soluble collagen; physicochemical; functional qualities

Full Text:

PDF

References


R. Gao, Q. Yu, Y. Shen, Q. Chu, G. Chen, S. Fen, M. Yang, L. Yuan, D. J. M. Clements, and Q. Sun “Production, bioactive properties, and potential applications of fish protein hydrolysates: Developments and challenges,†Trends in Food Science & Technology, vol. 110, pp. 687–699, 2021, doi: 10.1016/j.tifs.2021.02.031.

MYAgro, “Alu-Alu,†2020. http://portal.myagro.moa.gov.my/ms/dof/cfsh/Pages/Alu-Alu.aspx (accessed Apr. 24, 2021).

Z. Song, H. Liu, L. Chen, L. Chen, C. Zhou, P. Hong, and C. Deng “Characterization and comparison of collagen extracted from the skin of the Nile tilapia by fermentation and chemical pretreatment,†Food Chem, vol. 340, pp. 128139 2021, doi: 10.1016/j.foodchem.2020.128139.

S. N. H. Oslan, C. X. Li, R. Shapawi, R. A. M. Mokhtar, W. N. Md. Noordin, and N. Huda, “Extraction and characterization of bioactive fish by-product collagen as promising for potential wound healing agent in pharmaceutical applications: Current trend and future perspective,†International Journal Food Science, Article ID 9437878, 2022, doi: 10.1155/2022/9437878.

N. Baco, S. N. H. Oslan, R. Shapawi, R. A. M. Mohhtar, W. N. M. Noordin, and N. Huda, “Antibacterial activity of functional bioactive peptides derived from fish protein hydrolysate,†IOP Conference Series: Earth and Environmental Science, vol. 967, no. 1, pp. 012019, 2022, doi: 10.1088/1755-1315/967/1/012019.

Harianti, “Characterization chemical composition of skin and head bones barracuda (Sphyraena jello) as collagen raw material,†IOP Conference Series: Earth and Environmental Science, vol. 564, no. 1, p. 012046, 2020, doi: 10.1088/1755-1315/564/1/012046.

A. A. Jaziri, H. Hasanuddin, R. Shapawi, R. A. M. Mokhtar, W. N. M. Noordin, and N. Huda, “Nutritional composition and mineral analysis of the by-products from tropical marine fish, purple-spotted bigeye (Priacanthus tayenus Richardson, 1846) and barracuda (Sphyraena obtusata Cuvier, 1829),†IOP Conference Series: Earth and Environmental Science, vol. 967, no. 1, p. 012051, 2022, doi: 10.1088/1755-1315/967/1/012051.

J. Kuwahara, “Extraction of type i collagen from tilapia scales using acetic acid and ultrafine bubbles,†Processes, vol. 9, no. 2, pp. 1–11, 2021, doi: 10.3390/PR9020288.

M. H. Samiei, S. Jamili, H. Nikukar, and V. Razban, “Isolation, characterization and biocompatibility evaluation of collagen from Thunnus tonggol skin,†Iranian Journal of Fisheries Sciences, vol. 21, no. 2, pp. 568–589, 2022, doi: 10.22092/IJFS.2022.126579.

K. Nilsuwan, K. Fusang, P. Pripatnanont, and S. Benjakul, “Properties and Characteristics of Acid-Soluble Collagen from Salmon Skin Defatted with the Aid of Ultrasonication,†Fishes, vol. 7, no. 1, pp. 51, 2022, doi: 10.3390/FISHES7010051.

A. A. Jaziri, R. Shapawi, R. A. Mohd Mokhtar, W. N. Md. Noordin, and N. Huda, “Biochemical analysis of collagens from the bone of lizardfish (Saurida tumbil Bloch, 1795) extracted with different acids,†PeerJ, vol. 10, pp. e13103, 2022, doi: 10.7717/peerj.13103.

S. Srinivasan and B. Durairaj, “Collagen isolation and characterization from Sardinella longiceps,†Journal of Advanced Veterinary and Animal Research, vol. 8, no. 4, p. 679, 2021, doi: 10.5455/JAVAR.2021.H560.

T. M. T. Truong, V. M. Nguyen, T. T. Tran, and T. M. T. Le, “Characterization of acid-soluble collagen from food processing by-products of snakehead fish (Channa striata),†Processes, vol. 9, no. 7, pp. 1188, 2021, doi: 10.3390/PR9071188.

A. Abedinia, F. Ariffin, N. Huda, and A. M. Nafchi, “Preparation and characterization of a novel biocomposite based on duck feet gelatin as alternative to bovine gelatin,†International Journal of Biological Macromolecules, vol. 109, pp. 855-862. 2018, doi: 10.1016/j.ijbiomac.2017.11.051.

T. R. L. Senadheera, D. Dave, and F. Shahidi, “Sea Cucumber Derived Type I Collagen: A Comprehensive Review,†Mar Drugs, vol. 18, no. 9, pp. 471, 2020, doi: 10.3390/MD18090471.

H. Jafari, A. Lista, M. M. Siekapen, P. Ghaffari-Bohlouli, L. Nie, H. Alimoradi, and A. Shavandi, “Fish collagen: Extraction, characterization, and applications for biomaterials engineering,†Polymers, vol. 12, no. 10, pp. 1–37, 2020. doi: 10.3390/polym12102230.

R. Ahmed, M. Haq, and B. S. Chun, “Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus),†Int J Biol Macromol, vol. 135, pp. 668–676, 2019, doi 10.1016/j.ijbiomac.2019.05.213.

D. Yu, C. F. Chi, B. Wang, G. F. Ding, and Z. R. Li, “Characterization of acid-and pepsin-soluble collagens from spines and skulls of skipjack tuna (Katsuwonus pelamis),†Chinese Journal of Natural Medicines, vol. 12, no. 9, pp. 712–720, 2014, doi: 10.1016/S1875-5364(14)60110-2.

N. M. H. Khong, F. M. Yusoff, B. Jamilah, M. Basri, I. Maznah, K. W. Chan, N. Armania, and J. Nishikawa, “Improved collagen extraction from jellyfish (Acromitus hardenbergi) with increased physical-induced solubilization processes,†Food Chemistry, vol. 251, pp. 41–50, 2018, doi: 10.1016/j.foodchem.2017.12.083.

N. M. M. Hukmi and N. M. Sarbon, “Isolation and characterization of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) extracted from silver catfish (Pangasius sp.) skin,†International Food Research Journal, vol. 25, no. 6, pp. 2601-2607, 2018.

S. Nalinanon, S. Benjakul, W. Visessanguan, and H. Kishimura, “Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthus tayenus),†Food Chemistry, vol. 104, no. 2, pp. 593–601, 2007, doi: 10.1016/j.foodchem.2006.12.035.

J. Shon, J. B. Eun, J. H. Eo, and S. J. Hwang, “Effect of processing conditions on functional properties of collagen powder from skate (Raja kenojei) skins,†Food Science and Biotechnology 2011 20:1, vol. 20, no. 1, pp. 99–106, 2011, doi: 10.1007/S10068-011-0014-9.

M. Angel Martínez-Ortiz, A. Delia Hernández-Fuentes, D. J. Pimentel-González, R. G. Campos-Montiel, A. Vargas-Torres, and G. Aguirre-Ãlvarez, “Extraction and characterization of collagen from rabbit skin: partial characterization,†CyTA-Journal of Food, vol. 13, no. 2, pp. 253–258, 2015, doi: 10.1080/19476337.2014.946451.

I. Ismail, N. Huda, F. Ariffin, and R. Ahmad. “Effects of washing on the functional properties of duck meat,†International Journal of Poultry Science. vol. 9, no. 6, pp. 556-561, 2010. doi: 10.3923/ijps.2010.556.561.

AOAC, “Official methods of analysis of AOAC internationalâ€, 18th ed. Virginia, USA: Association of Official and Analytical Chemists International, 2006.

J. Wang, X. Pei, H. Liu, and D. Zhou, “Extraction and characterization of acid-soluble and pepsin-soluble collagen from skin of loach (Misgurnus anguillicaudatus),†International Journal of Biological Macromolecules, vol. 106, pp. 544–550, 2018, doi: 10.1016/j.ijbiomac.2017.08.046.

K. Matmaroh, S. Benjakul, T. Prodpran, A. B. Encarnacion, and H. Kishimura, “Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus),†Food Chemistry, vol. 129, no. 3, pp. 1179–1186, 2011, doi: 10.1016/j.foodchem.2011.05.099.

H. S. Jeong, J. Venkatesan, and S. K. Kim, “Isolation and characterization of collagen from marine fish (Thunnus obesus),†Biotechnology and Bioprocess Engineering, vol. 18, no. 6, pp. 1185–1191, 2013, doi: 10.1007/s12257-013-0316-2.

J. Chen, J. Li, Z. Li, R. Yi, S. Shi, K. Wu, Y. Li, and S. Wu, “Physicochemical and functional properties of type I collagens in red stingray (Dasyatis akajei) Skin,†Marine Drugs, vol. 17, no. 10, pp. 558, 2019, doi: 10.3390/md17100558.

A. N. Akram and C. Zhang, “Extraction of collagen-II with pepsin and ultrasound treatment from chicken sternal cartilage; physicochemical and functional properties,†Ultrasonics Sonochemistry, vol. 64, pp. 105053, 2020, doi: 10.1016/j.ultsonch.2020.105053.

R. Duan, J. Zhang, X. Du, X. Yao, and K. Konno, “Properties of collagen from skin, scale and bone of carp (Cyprinus carpio),†Food Chemistry, vol. 112, no. 3, pp. 702–706, 2009, doi: 10.1016/j.foodchem.2008.06.020.

M. Blanco, J. A. Vázquez, R. I. Pérez-Martín, and C. G. Sotelo, “Hydrolysates of fish skin collagen: an opportunity for valorizing fish industry byproducts,†Marine Drugs, vol. 15, no. 5, pp. 131, 2017, doi: 10.3390/MD15050131.

P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, T. Nagai, and M. Tanaka, “Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus),†Food Chemistry, vol. 89, no. 3, pp.363, 2015, doi: 10.1016/j.foodchem.2004.02.042.

N. Muralidharan, R. Jeya Shakila, D. Sukumar, and G. Jeyasekaran, “Skin, bone and muscle collagen extraction from the trash fish, leather jacket (Odonus niger) and their characterization,†Journal of Food Science and Technology, vol. 50, no. 6, pp. 1106, 2013, doi: 10.1007/S13197-011-0440-Y.

C. G. Sotelo, M. B. Comesaña, P. R. Ariza, and R. I. Pérez-Martín, “Characterization of collagen from different discarded fish species of the west coast of the Iberian Peninsula,†Journal of Aquatic Food Product Technology, vol. 25, no. 3, pp. 388–399, 2016, doi: 10.1080/10498850.2013.865283.

A. Sionkowska, K. Adamiak, K. Musial, and M. Gadomska, “Collagen based materials in cosmetic applications: A review,†Materials, vol. 13, no. 19, pp. 4217, 2020, doi: 10.3390/MA13194217.

N. H. Hadfi and N. M. Sarbon, “Physicochemical properties of silver catfish (Pangasius sp.) skin collagen as influenced by acetic acid concentration,†Food Research, vol. 3, no. 6, pp. 783–790, 2019, doi: 10.26656/FR.2017.3(6).130.

D. Liu, L. Liang, J. M. Regenstein, and P. Zhou, “Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (Hypophthalmichthys nobilis),†Food Chemistry, vol. 133, no. 4, pp. 1441–1448, 2012, doi: 10.1016/j.foodchem.2012.02.032.

Y. R. Huang, C. Y. Shiau, H. H. Chen, and B. C. Huang, “Isolation and characterization of acid and pepsin-solubilized collagens from the skin of balloon fish (Diodon holocanthus),†Food Hydrocolloids, vol. 25, no. 6, pp. 1507–1513, 2011, doi: 10.1016/j.foodhyd.2011.02.011.

P. Zhou, S. J. Mulvaney, and J. M. Regenstein, “Properties of Alaska pollock skin gelatin: A comparison with tilapia and pork skin gelatins,†Journal of Food Science, vol. 71, no. 6, pp. 313-321, 2006, doi: 10.1111/J.1750-3841.2006.00065.X.

A. A. Maktoof, R. Jafar Elherarlla, and S. Ethaib, “Identifying the nutritional composition of fish waste, bones, scales, and fins,†IOP Conference Series: Materials Science and Engineering, vol. 871, no. 1, pp. 012013, 2020, doi: 10.1088/1757-899X/871/1/012013.

A. da Trindade Alfaro, C. Simões Da Costa, G. Graciano Fonseca, and C. Prentice, “Effect of extraction parameters on the properties of gelatin from king weakfish (Macrodon ancylodon) bones,†Food Science and Technology International, vol. 15, no. 6, pp. 553–562, 2010, doi: 10.1177/1082013209352921.

J. Toppe, S. Albrektsen, B. Hope, and A. Aksnes, “Chemical composition, mineral content and amino acid and lipid profiles in bones from various fish species,†Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, vol. 146, no. 3, pp. 395–401, 2007, doi: 10.1016/j.cbpb.2006.11.020.

N. S. Sampath Kumar and R. A. Nazeer, “Characterization of acid and pepsin soluble collagen from the Skin of horse mackerels ( Magalaspis cordyla ) and croaker ( Otolithes ruber ),†International Journal of Food Properties, vol. 16, no. 3, pp. 613–621, 2013, doi: 10.1080/10942912.2011.557796.

N. Mohammad Reza, A. Maboud, and M. Zahra, “Isolation and purification of collagen from the skin of black pomfret (Parastromateus niger) for tissue engineering purpose,†Journal of Applied Tissue Engineering December, vol. 1, no. 1, pp. 18–21, 2014.

C. Li, W. Song, J. Wu, M. Lu, Q. Zhao, C. Fang, W. Wang, Y.D. Park, and G. Y. Qian, “Thermal stable characteristics of acid- and pepsin-soluble collagens from the carapace tissue of Chinese soft-shelled turtle (Pelodiscus sinensis),†Tissue Cell, vol. 67, pp. 101424, 2020, doi: 10.1016/J.TICE.2020.101424.

H. M. G. K. Herath, N. K. Kalutharage, and P. R. T. Cumaranatunga, “Solutions to an alien species invasion from aquarium aquaculture: Isolation and characterization of acid soluble collagen from sailfin catfish, Pterygoplichthys disjuctivus (Weber, 1991) in Sri Lanka,†Sri Lanka Journal of Aquatic Sciences, vol. 25, no. 1, pp. 19, 2020, doi: 10.4038/SLJAS.V25I1.7573.

T. Nagai, “Characterization of acid-soluble collagen from skins of surf smelt (Hypomesus pretiosus japonicus Brevoort),†Food and Nutrition Sciences, vol. 01, no. 02, pp. 59–66, 2010, doi: 10.4236/FNS.2010.12010.

M. Z. Abedin, A. A. Karim, F. Ahmed, A. A. Latiff, C. Y. Gan, F. Che Ghazali, and M.Z. Islam Sarker, “isolation and characterization of pepsin-solubilized collagen from the integument of sea cucumber (stichopus vastus),†Journal of the Science of Food and Agriculture, vol. 93, no. 5, pp. 1083–1088, 2013, doi: 10.1002/JSFA.5854.

Y. Tan and S. K. C. Chang, “Isolation and characterization of collagen extracted from channel catfish (Ictalurus punctatus) skin,†Food Chemistry, vol. 242, pp. 147–155, 2018, doi: 10.1016/j.foodchem.2017.09.013.

H. Abdelaal, “Characteristics of acid soluble collagen from catfish (Clarias Lazera) skin,†Annals of Agricultural Science, Moshtohor, vol. 59, no. 2, pp. 403–410, 2021, doi: 10.21608/ASSJM.2021.195006.

S. Tabarestani, Y. Maghsoudlou, A. Motamedzadegan, S. Mahoonak, and H. Rostamzad, “Study on some properties of acid-soluble collagens isolated from fish skin and bones of rainbow trout (Onchorhynchus mykiss),†International Food Research Journal, vol. 19, no. 1, pp. 251–257, 2012.

J. Chen, L. Li, R. Yi, N. Xu, R. Gao, and B. Hong, “Extraction and characterization of acid-soluble collagen from scales and skin of tilapia (Oreochromis niloticus),†LWT - Food Science and Technology, vol. 66, pp. 453–459, 2016, doi: 10.1016/J.LWT.2015.10.070.

S. Chen, H. Chen, Q. Xie, B. Hong, J. Chen, F. Hua, K. Bai, J. He, R. Yi, and H. Wu, “Rapid isolation of high purity pepsin-soluble type I collagen from scales of red drum fish (Sciaenops ocellatus),†Food Hydrocolloids, vol. 52, pp. 468–477, 2016, doi: 10.1016/j.foodhyd.2015.07.027.

Z. R. Li, B. Wang, C. Chi, Q. H. Zhang, Y. Gong, J. J. Tang, H. Luo, and G. Ding, “Isolation and characterization of acid soluble collagens and pepsin soluble collagens from the skin and bone of Spanish mackerel (Scomberomorous niphonius),†Food Hydrocolloids, vol. 31, no. 1, pp. 103–113, 2013, doi: 10.1016/j.foodhyd.2012.10.001.

S. Chuaychan, S. Benjakul, and H. Kishimura, “Characteristics of acid- and pepsin-soluble collagens from scale of seabass (Lates calcarifer),†LWT - Food Science and Technology, vol. 63, no. 1, pp. 71–76, 2015, doi: 10.1016/J.LWT.2015.03.002.

Y. Li, L. Yang, S. Wu, J. Chen, and H. Lin, “Structural, functional, rheological, and biological properties of the swim bladder collagen extracted from grass carp (Ctenopharyngodon idella),†LWT- Food Science and Technology, vol. 153, p. 112518, 2022, doi: 10.1016/J.LWT.2021.112518.

Y. Zou, L. Wang, P. Cai, P. Li, M. Zhang, Z. Sun, C. Sun, W. Xu, and D. Wang, “Effect of ultrasound assisted extraction on the physicochemical and functional properties of collagen from soft-shelled turtle calipash,†International Journal of Biological Macromolecules, vol. 105, no. 3, pp. 1602–1610, 2017, doi: 10.1016/j.ijbiomac.2017.03.011.

A. N. A. Aryee, D. Agyei, and C. C. Udenigwe, “Impact of processing on the chemistry and functionality of food proteins,†Proteins in Food Processing: Second Edition, pp. 27–45, 2018, doi: 10.1016/B978-0-08-100722-8.00003-6.




DOI: http://dx.doi.org/10.18517/ijaseit.13.2.18074

Refbacks

  • There are currently no refbacks.



Published by INSIGHT - Indonesian Society for Knowledge and Human Development