Gelation of Pangasius (Pangasianodon hypophthalmus) minced muscle by high pressure processing: The effects on selected qualities
, &
Article Sidebar
Main Article Content
Abstract
This study evaluated the changes of Pangasius hypophthalmus protein under high-pressure processing (HPP), focusing on key parameters such as color, gel structure, water-holding capacity (WHC), protein solubility, and mechanical properties to determine optimal conditions for improving product quality. Pangasius muscle were minced and subjected to pressures ranging from 100 to 600 MPa, at temperatures between 0 - 30°C, and for 0 - 15 min. The processed samples were then analyzed for color, gel texture, gel strength, WHC, protein solubility, scanning electron microscopy (SEM), fourier transform infrared spectroscopy (FTIR) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that treatment at 400 - 450 MPa enhanced the whiteness of Pangasius gels, improved microstructural texture, and increased water-holding capacity (WHC). In contrast, processing at 500 MPa at 30°C for 12.5 min reduced structural stability, led to the formation of porous networks, and decreased protein solubility. The gel’s mechanical properties were optimal at 400 - 450 MPa but reduced the hardness at 500 MPa. Overall, the conditions of 400 - 450 MPa, 20 - 30°C, and 10 - 15 min were identified as optimal for enhancing Pangasius gel quality.
Article Details
References
Buckow, R., & Bull, M. (2013). Advanced food preservation technologies. Microbiology Australia 34(2), 108-111.
Cando, D., Herranz, B., Borderías, A. J., & Moreno, H. M. (2015). Effect of high pressure on reduced sodium chloride surimi gels. Food Hydrocolloids 51, 176-187. https://doi.org/10.1016/j.foodhyd.2015.05.016.
Colmenero, F. J. (2002). Muscle protein gelation by combined use of high pressure/temperature. Trends in Food Science and Technology 13(1), 22-30. https://doi.org/10.1016/S0924-2244(02)00024-9.
Davis, J. S. (1985). Kinetics and thermodynamics of the assembly of the parallel-and antiparallelpacked sections of synthetic thick filaments of skeletal myosin: a pressure-jump study. Biochemistry 24(19), 5263-5269. https://doi.org/10.1021/bi00340a046.
de Oliveira, F. A., Neto, O. C., dos Santos, L. M. R., Ferreira, E. H. R., & Rosenthal, A. (2017). Effect of high pressure on fish meat quality - A review. Trends in Food Science and Technology 66, 1-19. https://doi.org/10.1016/j.tifs.2017.04.014.
Hwang, J. S., Lai, K. M., & Hsu, K. C. (2007). Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting. Food Chemistry 104(2), 746-753. http://dx.doi.org/10.1016/j.foodchem.2006.11.075.
Ikeuchi, Y., Tanji, H., Kim, K., & Suzuki, A. (1992). Mechanism of heat-induced gelation of pressurized actomyosin: Pressure-induced changes in actin and myosin in actomyosin. Journal of Agricultural and Food Chemistry 40(10), 1756-1761. https://doi.org/10.1021/jf00022a006.
Iwasaki, T., Noshiroya, K., Saitoh, N., Okano, K., & Yamamoto, K. (2006). Studies of the effect of hydrostatic pressure pretreatment on thermal gelation of chicken myofibrils and pork meat patty. Food Chemistry 95(3), 474-483.https://doi.org/10.1016/j.foodchem.2005.01.024.
Iwasaki, T., Washio, M., Yamamoto, K., & Nakamura, K. (2005). Rheological and morphological comparison of thermal and hydrostatic pressure-induced filamentous myosin gels. Journal of Food Science 70(7), e432-e436. https://doi.org/10.1111/j.1365-2621.2005.tb11472.x.
Kobayashi, Y., Mayer, S. G., & Park, J. W. (2017). FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under different comminution conditions. Food Chemistry 226, 156-164. https://doi.org/10.1016/j.foodchem.2017.01.068.
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.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. The Journal of Biological Chemistry 193(1), 265-275. https://doi.org/10.1016/S0021-9258(19)52451-6.
Ma, X. S., Yi, S. M., Yu, Y. M., Li, J. R., & Chen, J. R. (2015). Changes in gel properties and water properties of Nemipterus virgatus surimi gel induced by high-pressure processing. LWTFood Science and Technology 61(2), 377-384. https://doi.org/10.1016/j.lwt.2014.12.041.
Ojagh, S. M., Núñez-Flores, R., López-Caballero, M. E., Montero, M. P., & Gómez-Guillén, M. C. (2011). Lessening of high-pressure-induced changes in Atlantic salmon muscle by the combined use of a fish gelatin–lignin film. Food Chemistry 125(2), 595-606. http://dx.doi.org/10.1016/j.foodchem.2010.08.072.
Pazos, M., Méndez, L., Vázquez, M., & Aubourg, S. P. (2015). Proteomics analysis in frozen horse mackerel previously high-pressure processed. Food Chemistry 185, 495-502. https://doi.org/10.1016/j.foodchem.2015.03.144.
Ramírez, J. A., Martín-Polo, M. O., & Bandman, E. (2000). Fish myosin aggregation as affected by freezing and initial physical state. Journal of Food Science 65(4), 556-560. https://doi.org/10.1111/j.1365-2621.2000.tb16047.x.
Sikes, A. L., Tobin, A. B., & Tume, R. K. (2009). Use of high pressure to reduce cook loss and improve texture of low-salt beef sausage batters. Innovative Food Science and Emerging Technologies 10(4), 405-412. https://doi.org/10.1016/j.ifset.2009.02.007.
Tabilo-Munizaga, G., & Barbosa-Cánovas, G. V. (2004). Ultra high pressure technology and its use in surimi manufacture: An overview. Food Science and Technology International 10(4), 207-222. https://doi.org/10.1177/1082013204045687.
Truong, B. Q., Buckow, R., & Nguyen, M. (2020). Mechanical and functional properties of unwashed barramundi (Lates calcarifer) gels as affected by high-pressure processing at three different temperatures and salt concentrations. Journal of Aquatic Food Product Technology 29(4), 373-382. https://doi.org/10.1080/10498850.2020.1739792.
Truong, B. Q., Buckow, R., Nguyen, M. H., & Furst, J. (2017). Gelation of barramundi (Lates calcarifer) minced muscle as affected by pressure and thermal treatments at low salt concentration. Journal of the Science of Food and Agriculture 97(11), 3781-3789. https://doi.org/10.1002/jsfa.8242.
Uresti, R. M., Velazquez, G., Ramírez, J. A., Vázquez, M., & Torres, J. A. (2005). Effect of high-pressure treatments on mechanical and functional properties of restructured products from arrowtooth flounder (Atheresthes stomias). Journal of The Science of Food and Agriculture 84(13), 1741-1749. https://doi.org/10.1002/jsfa.1876.
Ye, T., Dai, H., Lin, L., & Lu, J. (2019). Employment of κ-carrageenan and high pressure processing for quality improvement of reduced NaCl surimi gels. Journal of Food Processing and Preservation 43(9), e14074. https://doi.org/10.1111/jfpp.14074.