Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin

被引:194
作者
Hu, Hao [1 ,2 ,3 ]
Cheung, Imelda W. Y. [2 ]
Pan, Siyi [1 ,3 ]
Li-Chan, Eunice C. Y. [2 ]
机构
[1] Huazhong Agr Univ, Coll Food Sci & Technol, Wuhan 430070, Hubei, Peoples R China
[2] Univ British Columbia, Fac Land & Food Syst, Food Nutr & Hlth Program, Vancouver, BC V6T 1Z4, Canada
[3] Huazhong Agr Univ, Minist Educ, Key Lab Environm Correlat Dietol, Wuhan, Peoples R China
关键词
High intensity ultrasound; Soy beta-conglycinin; Soy glycinin; Emulsifying properties; Physicochemical properties; SOY PROTEIN ISOLATE; STRUCTURAL CHARACTERISTICS; PHYSICAL-PROPERTIES; POWER ULTRASOUND; DISULFIDE BONDS; GLOBULIN; FRACTIONATION; SULFHYDRYL; GELATION; MILK;
D O I
10.1016/j.foodhyd.2014.11.004
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The effects of high intensity ultrasound treatment (HUS; 20 kHz at 400 W for 5, 20 or 40 min) on aggregated soybean beta-conglycinin (7S) and glycinin (11S) fractions were investigated in this study. HUS decreased turbidity and particle size of 7S in 0.05 M Tris-HCl buffer at pH 7.0, while it increased surface hydrophobicity (H-0), solubility, emulsifying activity (EAI) and emulsion stability (ESI). Similarly, HUS of soybean 11S decreased turbidity while increasing EAI but it had minimal effects on particle size and ESI. The SH groups of both 7S and 11S fractions decreased after HUS. HUS did not change 7S or 11S secondary structure, but it slightly increased the percentage of high molecular-weight aggregates under non-reducing SDS-PAGE, and changed the microenvironment of aromatic and aliphatic side chains as observed by Raman spectroscopy of freeze-dried samples. These findings on physicochemical changes of 11S and especially of 7S proteins induced by HUS treatment may contribute to improved applications of soy proteins in food products. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:102 / 110
页数:9
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