Effect of Low Pressure Homogenization on Solubility and Structure of Soybean Protein Isolate

被引：0
|
作者：
Li Y. [1 ]
Li M. [1 ]
Zhang Y. [1 ]
Jiang L. [1 ]
Wang Z. [1 ]
Teng F. [1 ]
机构：
[1] College of Food Science, Northeast Agricultural University, Harbin
来源：
Nongye Jixie Xuebao/Transactions of the Chinese Society for Agricultural Machinery | 2019年 / 50卷 / 03期
关键词：
Emulsification; Low pressure homogenization; Solubility; Soybean protein isolate;
D O I：
10.6041/j.issn.1000-1298.2019.03.039
中图分类号：
学科分类号：
摘要：
High pressure homogenization is one of the most common physical modification methods in protein processing. However, the pressure of homogenization generally does not exceed 40 MPa in actual production due to the limitation of equipment. Therefore, it is of great importance to study the effect of low pressure homogenization (0~40 MPa) on the solubility and structure of soybean protein isolate. The effects of low-pressure homogenization (0~40 MPa) on the solubility and structure of soybean protein isolate (SPI) were studied by measuring particle size distribution, solubility, emulsification, tertiary structure and thermal stability. The results showed that low-pressure homogenization treatment could reduce the particle size of SPI, significantly improve the solubility, and the solubility was positively correlated with emulsifying ability and emulsifying stability. The linear fitting model functions were obtained, and the correlation coefficients were 0.956 8 and 0.962 5, respectively. Fluorescence spectrum analysis showed that the structure of SPI was expanded with the increase of homogeneous pressure, the maximum absorption wavelength was red-shifted, the internal tryptophan group was exposed, and the fluorescence intensity was increased with the increase of homogeneous pressure. At 30 MPa, the fluorescence intensity was the highest. When homogeneous pressure was further increased, the protein molecules were aggregated, and the former exposed active groups were hided in the inside of SPI with a slight decrease in fluorescence intensity due to inward crimping of active groups. The above results were verified by the analysis results of thermal stability. © 2019, Chinese Society of Agricultural Machinery. All right reserved.
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页码：345 / 351
页数：6
相关论文
共 30 条
  • [1] Jiang L., An introduction of the flexible processing technology of edible protein, Journal of Chinese Institute of Food Science and Technology, 15, 8, pp. 1-9, (2015)
  • [2] Zhai A., Yang S., The influence of high pressure homogenization on the functional properties of 7S and 11S, Food Science and Technology, 6, pp. 208-211, (2015)
  • [3] Yang S., Zhai A., Effect of high pressure homogenization on functional properties of soy protein isolate, Chinese Brewing, 33, 12, pp. 89-93, (2014)
  • [4] Yang J., Liu G., Zeng H., Et al., Effects of high pressure homogenization on faba bean protein aggregation in relation to solubility and interfacial properties, Food Hydrocolloids, 83, 1, pp. 275-284, (2018)
  • [5] Yu C., Wu F., Yue C., Et al., Effects of high-pressure homogenization on functional properties and structure of mussel (Mytilus edulis) myofibrillar proteins, International Journal of Biological Macromolecules, 118, pp. 741-746, (2018)
  • [6] Zhang Y., Jiang F., Liu Q., Et al., The changes of emulsify properties of soybean protein isolate induced by ultra high pressure homogenization, Food Research and Development, 38, 1, pp. 1-5, (2017)
  • [7] Wang C., Jiang L., Wei D., Et al., Relationship between structure and surface hydrophobicity of soybean protein isolates from different varieties, Food Science, 33, 9, pp. 54-57, (2012)
  • [8] Tang S., Hettiarachchy N.S., Horax R., Et al., Physicochemical properties and functionality of rice bran protein hydrolyzate prepared from heat-stabilized defatted rice bran with the aid of enzymes, Journal of Food Science, 68, 1, pp. 152-157, (2003)
  • [9] Tang C., Yang X., Chen Z., Et al., MTGase polymerization of soybean protein and its modification mechanism (Ⅲ) mtgase polymerization modified soy protein mechanism, Chinese Journal of Grain and Oil, 19, 3, pp. 42-46, (2004)
  • [10] Zhang H.M., Wang Y.Q., Jiang M.L., A fluorimetric study of the interaction of C. I. Solvent Red 24 with haemoglobin, Dyes &Pigments, 82, 2, pp. 156-163, (2009)
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