Effect of Pressurized Soy Protein Isolate upon the Growth and Antioxidants Functions of SD Rat


The objective of this study is to specify the effect of pressurized soy protein isolate (pSPI), upon the physical development, growth hormones and antioxidants functions of SD rats. The methodology depends on the selection of one hundred male SD rats, divided randomly into 5 groups. Each group consists of 20 rats. The groups will be defined as one blank control group, three groups with pSPI at low, medium and high doses and another control group with native soy protein isolates (nSPI). Low, medium and high doses are represented by 0.333 g/kg, 1.667 g/kg and 3.333 g/kg pSPI per weight, respectively. The native soy protein isolate is represented by 3.333 g/kg nSPI per weight. In every group, four animals will be taken out to collect the blood samples and analyze insulin like growth factor-I, growth hormone, thyroid stimulating hormone, thyroxine and triiodothyronin. The other SD rats will be subjected to feeding for 63 consecutive days. The body weight, the body length and food intake of each rat are measured. The total antioxidant capacity, superoxide dismutase (SOD), malondialdehyde and Glutathione Peroxidase in liver and serum of each rat will be analyzed. The results indicated that the groups with medium and high dose of pSPI result in an obvious increase in the body weight, body length and food utilization rate of SD rats. Also, pSPI has a great effect on the growth and antioxidants functions of SD rat.

Share and Cite:

Ali, N. , Zhang, L. , Li, L. , Chan, L. and Li, B. (2015) Effect of Pressurized Soy Protein Isolate upon the Growth and Antioxidants Functions of SD Rat. Food and Nutrition Sciences, 6, 501-510. doi: 10.4236/fns.2015.65052.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] Nishinari, K. (1988) Food hydrocolloids in Japan. National Food Research Institute, Tsukuba.
[2] Peng, I.C., Quass, D.W., Dayton, W.R. and Allen, C.E. (1984) Physicochemical and Functional Properties of Soybean 11S Globulin—A Review. Cereal Chemistry, 61, 480-490.
[3] Molina, E., Papadopoulou, A. and Ledward, D.A. (2001) Emulsifying Properties of High Pressure Treated Soy Protein Isolate and 7S and 11S Globulins. Food Hydrocolloids, 15, 263-269.
[4] Puppo, C. and Chapleau, N. (2004) Physicochemical Modifications of High-Pressure-Treated Soybean Protein Isolates. Food Chemistry, 52, 1564-1571.
[5] Takenaka, A. and Annaka, H. (2003) Reduction of Paraquat-Induced Pxidative Stress in Rat by Dietary Soy Peptide. Bioscience Biotechnology and Biochemistry, 67, 278-283.
[6] Wu, W., Zhang, C. and Hua, Y. (2009) Structural Modification of Soy Protein by the Lipid Peroxidation Product Malondialdehyde. Journal of the Science of Food and Agriculture, 89, 1416-1423.
[7] Anderson, J., Johnstone, B. and Cook-Newell, M. (1995) Meta-Analysis of the Effects of Soy Protein Intake on Serum Lipids. England Journal of Medicine, 333, 276-282.
[8] Hashizume, K. and Watababe, T. (1979) Influence of Heating Temperature on Conformational Changes of Soybean Proteins. Agricultural and Biological Chemistry, 43, 683-690.
[9] Zhang, H., Li, L., Tatsumi, E. and Kotwal, S. (2003) Influence of High Pressure on Conformational Changes of Soybean Glycinin. Innovative Food Science and Emerging Technologies, 4, 269-275.
[10] Speroni, F., Beaumal, V., Lamballerie, Md., Anton, M., Anona, M.C. and Puppo, M.C. (2009) Gelation of Soybean Proteins Induced by Sequential High-Pressure and Thermal Treatments. Food Hydrocolloids, 23, 1433-1442.
[11] Song, X., Zhoub, C., Fuc, F., Chenc, Z. and Wub, Q. (2013) Effect of High-Pressure Homogenization on Particle Size and Film Properties of Soy Protein Isolate. Industrial Crops and Products, 43, 538-544.
[12] Speroni, F., Anón, M.C. and Lamballerie, M.D. (2010) Effects of Calcium and High Pressure on Soybean Proteins: A Calorimetric Study. Food Research International, 43, 1347-1355.
[13] Gupta, S., Hevia, D., Patchva, S., Park, B., Koh, W. and Aggarwal, B. (2012) Upsides and Downsides of Reactive Oxygen Species for Cancer: The Roles of Reactive Oxygen Species in Tumorigenesis, Prevention, and Therapy. Antioxidants & Redox Signaling, 16, 1295-1322.
[14] Turrens, J. (2003) Mitochondrial Formation of Reactive Oxygen Species. Journal of Physiology, 552, 335-344.
[15] Orozco, R.F., Piskula, M.K., Zielinski, H., Kozlowska, H., Frias, J. and Vidal-Valverde, C. (2006) Germination as a Process to Improve the Antioxidant Capacity of Lupinus angustifolius L. var. Zapaton. European Food Research and Technology, 223, 495-502.
[16] Zielinska, D., Frias, J., Piskula, M.K., Kozlowska, H., Zielinsk, H. and Vidal-Valverde, C. (2008) Evaluation of the Antioxidant Capacity of Lupin Sprouts Germinated in the Presence of Selenium. European Food Research and Technology, 227, 1711-1720.
[17] Hengst, C., Werner, S., Müller, L., Frohlich, K. and Bohm, V. (2009) Determination of the Antioxidant Capacity: Influence of the Sample Concentration on the Measured Values. European Food Research and Technology, 230, 249-254.
[18] Zhang, Y., Du, R., Wang, L. and Zhang, H. (2010) The Antioxidative Effects of Probiotic Lactobacillus casei Zhang on the Hyperlipidemic Rats. European Food Research and Technology, 231, 151-158.
[19] Maki, R.G. (2010) Small Is Beautiful: Insulin-Like Growth Factors and Their Role in Growth, Development, and Cancer. Journal of Clinical Oncology, 28, 4985-4995.
[20] Townsend, D. and Tew, K. (2003) The Role of Glutathione-S-Transferase in Anti-Cancer Drug Resistance. Oncogene, 22, 7369-7375.

Copyright © 2023 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.