Page Header

Effect of Cryoprotectants on Quality of Desalted Jellyfish Subjected to Multiple Freeze- Thaw Cycles

Wiriya Charoenchokpanich, Pratchaya Muangrod, Benjawan Thumthanaruk, Vilai Rungsardthong, Savitri Vatanyoopaisarn, Benjamaporn Wonganu, Sittiruk Roytrakul


A freeze-thaw cycle in frozen products occurs when the temperature fluctuates during storage or transportation, causing drip loss, changes in ice crystal reformation, and textural protein. In practical freezing, using cryoprotectants in frozen products aids in delaying the physicochemical changes. The problem has been found in commercial frozen jellyfish with sesame oil, causing the separating oil and water derived from drip loss of thawed jellyfish protein. This study aimed to select an appropriate cryoprotectant and concentration for frozen jellyfish products. Therefore, this research compared the changes in the physical and textural properties of desalted jellyfish collagen protein soaked in inulin, sucrose, or sorbitol at 1, 5, and 10% and subjected to three freeze-thaw cycles. Results showed increased concentration of each cryoprotectant increased soaking yield. The maximum soaking yields of desalted jellyfish were 2.49 ± 0.54, 2.79 ± 0.82, and 2.78 ± 0.51%, and each cryoprotectant content was 7.18 ± 0.01, 7.54 ± 0.00, and 8.58 ± 0.32% when using static soaked in inulin, sucrose, and sorbitol at 10%. During the freeze-thaw cycle, the retardation of the denatured jellyfish protein from ice crystals increased when desalted jellyfish were immersed in inulin, sucrose, or sorbitol at the maximum concentration of 10%, displaying the drip losses at 27.88 ± 0.45, 29.45 ± 0.35, and 28.56 ± 0.73% that lowered than the control at 56.54 ± 0.64%. The increased repeated freeze-thaw cycles increased the compact structure of thawed jellyfish collagen, supported by microstructure analysis. In summary, inulin at 10% appears to have a cryoprotective effect similar to sucrose and sorbitol and will be a choice for commercial frozen jellyfish-based food menu development.


[1] H. E. Ramírez-Guerra, C. O. García-Sifuentes, R. Pacheco-Aguilar, J. C. Ramirez-Suarez, M. E. Lugo-Sánchez, and S. M. Scheuren-Acevedo, “The influence of ante-mortem hypoxia on the physicochemical stability of myofibrillar proteins in the muscle tissue of white shrimp (Litopenaeus vannamei) exposed to multiple freeze–thaw cycles,” European Food Research and Technology, vol. 235, pp. 37–45, Jul. 2012, doi: 10.1007/ s00217-012-1702-2.


[2] B. Zhang, H. Yao, H. Qi, and X. G. Ying, “Cryoprotective characteristics of different sugar alcohols on peeled Pacific white shrimp (Litopenaeus vannamei) during frozen storage and their possible mechanisms of action,” International Journal of Food Properties, vol. 23, no. 1, pp. 95–107, Jan. 2020, doi: 10.1080/10 94291 2.2019.1710533.


[3] M. D. Alvarez, C. Fernández, and W. Canet, “Oscillatory rheological properties of fresh and frozen/thawed mashed potatoes as modified by different cryoprotectants,” Food and Bioprocess Technology, vol. 3, pp. 55–70, Feb. 2010, doi: 10.1007/s11947-007-0051-9.


[4] S. Bolliger, H. Wildmoser, H. D. Goff, and B. Tharp, “Relationships between ice cream mix viscoelasticity and ice crystal growth in ice cream,” International Dairy Journal, vol. 10, no. 11, pp. 791–797, 2000, doi: 10.1016/S0958-6946 (00)00108-4.


[5] N. Rattanasatheirn, S. Benjakul, W. Visessanguan, and K. Kijroongrojana, “Properties, translucence, and microstructure of Pacific white shrimp treated with mixed phosphates as affected by freshness and deveining,” Journal of Food Science, vol. 73, no. 1, pp. S31–S40. 2008, doi: 10.1111/j.17 50-3841.2007.00603.x.


[6] F. Erdogdu, M. O. Balaban, W. S. Otwell, and L. Garrido, “Cook-related yield loss for pacific white (Penaeus vannamei) shrimp previously treated with phosphates: effects of shrimp size and internal temperature distribution,” Journal of Food Engineering, vol. 64, no. 3, pp. 297–300, Sep. 2004, doi: 10.1016/j.jfoodeng.2003.10.012.


[7] M. J. Torti, C. A. Sims, C. M. Adams, and P. J. Sarnoski, “Polysaccharides as alternative moisture retention agents for shrimp,” Journal of Food Science, vol. 81, no. 3, pp. S728–S735, Mar. 2016, doi: 1111/1750-3841.13242.


[8] X. Chen, J. Wu, X. Li, F. Yang, L. Yu, X. Li, J. Huang, and S. Wang, “Investigation of the cryoprotective mechanism and effect on quality characteristics of surimi during freezing storage by antifreeze peptides,” Food Chemistry, vol. 371, Mar. 2022, Art. no. 131054, doi: 10.1016/j. foodchem.2021.131054.


[9] M. M. English, P. M. Scrosati, A. J. Aquino, M. B. McSweeney, and M. S. G. Razul, “Novel carbohydrate blend enhances chemical and sensory properties of lobster (Homarus americanus) after one-year frozen storage,” Food Research International, vol. 137, Nov. 2020, Art. no. 109697, doi: 10.1016/j.foodres.2020. 109697.


[10] K. Wachirasiri, S. Wanlapa, D. Uttapap, and V. Rungsardthong, “Use of amino acids as a phosphate alternative and their effects on quality of frozen white shrimps (Penaeus vanamei),” LWT-Food Science and Technology, vol. 69, pp. 303–311, Jun. 2016, doi: 10.1016/ j.lwt.2016.01. 065.


[11] K. A. Thorarinsdottir, G. Gudmundsdottir, S. Arason, G. Thorkelsson, and K. Kristbergsson, “Effects of added salt, phosphates, and proteins on the chemical and physicochemical characteristics of frozen cod (Gadus morhua) fillets,” Journal of Food Science, vol. 69, no. 4, pp. SNQ144– SNQ152, May 2004, doi: 10.1111/ j.1365- 2621.2004.tb06355.x.


[12] Y. Li, B. Kong, X. Xia, Q. Liu, and P. Li, “Inhibition of frozen storage‐induced oxidation and structural changes in myofibril of common carp (Cyprinus carpio) surimi by cryoprotectant and hydrolysed whey protein addition,” Journal of Food Science & Technology, vol. 48, no. 9, pp. 1916–1923, Sep. 2013, doi: 10.1111/ijfs.12171.


[13] M. Baldini, F. Danuso, A. Rocca, E. Bulfoni, M. T. Amaducci, A. Monti, and G. D. Mastro, “Jerusalem artichoke (Helianthus tuberosus L.) productivity in different Italian growing areas: A modelling approach,” Italian Journal of Agronomy, vol. 6, no. 2, pp. 126–132, 2011, doi:10.4081/ ija.2011.e20.


[14] A. Franck, “Technological functionality of inulin and oligofructose,” British Journal of Nutrition, vol. 87, pp. S287–S291, May 2002, doi: 10.1079/ BJN/2002550.


[15] J. Ye, R. Yang, C. Liu, S. Luo, J. Chen, X. Hu, and J. Wu, “Improvement in freeze-thaw stability of rice starch gel by inulin and its mechanism,” Food Chemistry, vol. 268, pp. 324–333, Dec. 2018, doi: 10.1016/j.foodchem.2018.0 6.086.


[16] Y. Cao, L. Zhao, Q. Huang, S. Xiong, T. Yin, and Z. Liu, “Water migration, ice crystal formation, and freeze-thaw stability of silver carp surimi as affected by inulin under different additive amounts and polymerization degrees,” Food Hydrocolloids, vol. 124, Mar. 2022, Art. no. 107267, doi: 10.1016/j.foodhyd.2021.107267.


[17] Y. H. P. Hsieh, F. M. Leong, and J. Rudloe, “Jellyfish as food,” Hydrobiologia, vol. 451, no. 1, pp. 11–17, May 2001, doi: 10.1023/ A:1011875 720415.


[18] T. Klaiwong, P. Hutangura, S. Rutatip, P. Wongsa- Ngasri, and B. Thumthanaruk, “Comparative properties of pepsin hydrolyzed jellyfish protein from salted jellyfish,” Journal of Agricultural Science and Technology B, vol. 4, no. 7, pp. 555–564, Jul. 2014, doi: 10.17265/2161- 6264/2014.07.005.


[19] M. T. Pedersen and T. A. Vilgis, “Soft matter physics meets the culinary arts: From polymers to jellyfish,” Journal of Gastronomy and Food Science, vol. 16, Jul. 2019, Art. no. 10013, doi: 10.1016/j.ijgfs.2019.100135.


[20] J. R. Li and Y. H. P. Hsieh, “Traditional Chinese food technology and cuisine,” Asia Pacific Journal of Clinical Nutrition, vol. 13, no. 2, pp. 147–155, Jun. 2004.


[21] W. Charoenchokpanich, V. Rungsardthong, S. Vatanyoopaisarn, B. Thumthanaruk, and Y. Tamaki, “Salt reduction in salted jellyfish (Lobonema smithii) using a mechanical washing machine,” Science, Engineering and Health Studies, vol. 14, no. 3, pp. 184–192, Sep. 2020, doi: 10.14456/sehs.2020.17.


[22] P. Muangrod, V. Rungsardthong, S. Vatanyoopaisarn, Y. Tamaki, E. Kuraya, and B. Thumthanaruk, “Effect of wash cycle on physical and chemical properties of rehydrated jellyfish by-products and jellyfish protein powder,” Science, Engineering and Health Studies, vol. 15, Mar. 2021, Art. no. 21030004, doi: 10.14456/ sehs.2021.14.


[23] AOAC, Official Method of Analysis: Association of Analytical Chemists, 19th ed. Washington, D.C.: AOAC International, pp. 121–130, 2012.


[24] P. Wongsa-ngasri, P. Virulhakul, and B. Thumthanaruk, “Study of salted jellyfish production in commercial,” in The Annual Conference on Fisheries, pp. 284–297, 2008.


[25] M. T. Pedersen, J. R. Brewer, L. Duelund, and P. L. Hansen, “On the gastrophysics of jellyfish preparation,” International Journal of Gastronomy and Food Science, vol. 9, pp. 34–38, Oct. 2017, doi: 10.1016/j.ijgfs.2017.04.001.


[26] R. Usha, S. S. Raman, V. Subramanian, and T. Ramasami, “Role of polyols (erythritol, xylitol and sorbitol) on the structural stabilization of collagen,” Chemical Physics Letters, vol. 430, no. 4–6, pp. 391–396, Oct. 2006, doi: 10.1016/ j.cplett.2006.09.023.


[27] H. D. Belitz, W. Grosch, P. Schieberle, Food Chemistry, 4th ed. Berlin, Germany: Springer- Verlag Berlin Heidelberg, 2009.


[28] S. Boonsumrej, S. Chaiwanichsiri, S. Tantratian, T. Suzuki, and R. Takai, “Effects of freezing and thawing on the quality changes of tiger shrimp (Penaeus monodon) frozen by air-blast and cryogenic freezing,” Journal of Food Engineering, vol. 80, no. 1, pp. 292–299, May 2007, doi: 10.1016/j.jfoodeng.2006.04.059.


[29] S. Benjakul and F. Bauer, “Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze–thaw cycles,” Journal of the Science of Food and Agriculture, vol. 80, no. 8, pp. 1143–1150, Jun. 2000, doi: 10.1002/1097-0010(200006)80:8.


[30] P. U. S. George, “Influence of cryoprotectant levels on storage stability of surimi from Nemipterus japonicus and quality of surimi-based products,” Journal of Food Science and Technology, vol. 51, no. 5, pp. 982–987, May 2014, doi: 10.1007/ s13197-011-0590-y.


[31] J. F. Carpenter and J. H. Crowe, “The mechanism of cryoprotection of proteins by solutes,” Cryobiology, vol. 25, no. 3, pp. 244–255, Jun.1988, doi: 10.1016/0011-2240(88)90032-6.


[32] J. Li, J. Chen, L. An, X. Yuan, and L. Yao, “Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function” Communications Biology, vol. 3, p. 528, Sep. 2020, doi:/10.1038/s42003-020-01260-1.

Full Text: PDF

DOI: 10.14416/j.asep.2023.11.001


  • There are currently no refbacks.