Structure and Molecular Weight Distribution in Vitro Digestion Products of Soy Protein at Different Heat Treatment Conditions

被引：0
|
作者：
Zhao C. [1 ]
Yin H. [1 ]
Yan J. [1 ]
Liu J. [1 ]
Du C. [1 ]
Niu X. [1 ]
Qi B. [2 ]
机构：
[1] College of Food Science and Engineering, Jilin Agricultural University, National Engineering Laboratory for Wheat and Corn Deep Processing, Changchun
[2] College of Food Science, Northeast Agricultural University, Harbin
来源：
Qi, Baokun (qibaokun2016@163.com) | 1600年 / Chinese Institute of Food Science and Technology卷 / 20期
关键词：
Heat treatment; In vitro digestion; Molecular weight distribution; Soy protein; Structure;
D O I：
10.16429/j.1009-7848.2020.05.008
中图分类号：
学科分类号：
摘要：
Pepsin was used for in vitro simulated digestion of heat-treated soybean protein isolate (SPI). The subunit composition, protein secondary structure and molecular weight distribution of digestion products were researched. The degree of hydrolysis increased firstly and then decreased with the increase of heat treatment temperature and time, which indicated that proper heat treatment conditions could promote the digestion and degradation of SPI by pepsin. The heat treatment was able to change in vitro digestion mode of SPI, reducing the digestion degree of 11S subunit, leading to the digestion and degradation of 7S subunits, which formed the component with the molecular weight lower than 17 ku. Heat treatment mainly resulted in the increase of α-helix content and the decrease of β-sheet content in the secondary structure of digestion products. The molecular weight distribution of SPI digestion products was also changed. As rising of heat treatment temperature, the α-helix content increased firstly and then decreased, whereas the opposite trend was noted for β-sheet content. However, the heat treatment time had no significant effect on the content of all secondary structures. For the SPI digestion products, high temperature or heat treatment for long time could increase the distribution in the range of more than 100 ku and 3-10 ku, while decrease the distribution in the range of 10-100 ku and less than 3 ku. © 2020, Editorial Office of Journal of CIFST. All right reserved.
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页码：59 / 65
页数：6
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共 21 条
  • [1] Utsumi S., Maruyama N., Satoh R., Et al., Structure-function relationships of soybean proteins revealed by using recombinant systems, Enzyme and Microbial Technology, 30, 3, pp. 284-288, (2002)
  • [2] Kinsella J.E., Functional properties of soy proteins for food applications, Journal of the American Oil Chemists' Society, 56, pp. 242-258, (1979)
  • [3] Ragab D.D.M., Babiker E.E., Eltinay A.H., Et al., Fractionation, solubility and functional properties of cowpea(Vigna unguiculata) proteins as affected by pH and/or salt concent ration, Food Chemistry, 84, 2, pp. 207-212, (2004)
  • [4] Abdel-Aal E.S.M., Effects of baking on protein digestibility of organic spelt products determined by two in vitro digestion methods, LWT-Food Science and Technology, 41, 7, pp. 1282-1288, (2008)
  • [5] Moreno F.J., Quintanilla-Lopez J.E., Lebron-Aguilar R., Et al., Mass spectrometric characterization of glycated β-lactoglobulin peptides derived from galacto-oligosaccharides surviving the in vitro gastointestinal digestion, Journal of the American Society for Mass Spectrometry, 19, 7, pp. 927-937, (2008)
  • [6] Hu A.J., Zheng J., Comparison of enzymatic hydrolysis technologies of soybean protein, Fine Chemical Engineering, 22, 6, pp. 461-463, (2005)
  • [7] Tang C.H., Chen L., Ma C.Y., Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: a comparative study, Food Chemistry, 113, 4, pp. 957-963, (2009)
  • [8] Petruccelli S., Anon M., Relationship between the method of obtention and the structural and functional properties of soy proteins isolates. 1. Structural and Hydration properties, Journal of Agricultural and Food Chemistry, 42, 10, pp. 2161-2169, (1994)
  • [9] Zhang S., Vardhanabhuti B., Effect of initial protein concentration and pH on in vitro gastric digestion of heated whey proteins, Food Chemistry, 145, 2, pp. 473-480, (2014)
  • [10] Adler-Nissen J., Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid, Journal of Agricultural and Food Chemistry, 27, 6, pp. 1256-1262, (1979)
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