Effect of partial replacement of water-soluble cod proteins by soy proteins on the heat-induced aggregation and gelation properties of mixed protein systems

被引:89
作者
Wu, Chao [1 ]
Wang, Jiamei [1 ]
Yan, Xinyu [1 ]
Ma, Wuchao [1 ]
Wu, Di [1 ]
Du, Ming [1 ]
机构
[1] Dalian Polytech Univ, Sch Food Sci & Technol, Collaborat Innovat Ctr Prov & Minist Coconstruct, Natl Engn Res Ctr Seafood, Dalian 116034, Peoples R China
关键词
Mixed protein; Soy proteins; Water soluble cod proteins; Aggregation; Gelation; RHEOLOGICAL PROPERTIES; BETA-CONGLYCININ; NETWORK PROTEINS; IONIC-STRENGTH; TEMPERATURE; GLYCININ; GLOBULIN; BEHAVIOR; GELS; PH;
D O I
10.1016/j.foodhyd.2019.105417
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The interest for partially replacing animal proteins by plant proteins is growing. However, this is challenged by the arising negative effects on textural properties of the animal protein systems induced by the partial replacement. In this study, we investigated the aggregation behavior and mechanical properties of gels prepared with mixtures of water-soluble cod proteins (CPs) and preheated soy proteins (SPs) with different 7S/11S ratio. Results revealed that higher 11S ratio in the mixture resulted aggregates with larger size, higher surface hydrophobicity, and more disulfide bonds, affording the formation of porous network with higher storage modulus. In addition, rheological and microstructural results evidenced that the gel cross-linking was markedly strengthened when SPs were preheated and also dependent on temperature and protein concentration. The present study demonstrated the successful preparation of mixed protein gels with desirable rheological and microstructural properties, which was achieved by simply altering the 7S/11S ratio or preheating of SPs fraction. Additionally, these findings may provide fundamental knowledge for structuring food products based on mixed protein system.
引用
收藏
页数:9
相关论文
共 45 条
[1]   Micro-phase separation explains the abrupt structural change of denatured globular protein gels on varying the ionic strength or the pH [J].
Ako, Komla ;
Nicolai, Taco ;
Durand, Dominique ;
Brotons, Guillaume .
SOFT MATTER, 2009, 5 (20) :4033-4041
[2]   DETERMINATION OF SH-GROUPS AND SS-GROUPS IN SOME FOOD PROTEINS USING ELLMANS REAGENT [J].
BEVERIDGE, T ;
TOMA, SJ ;
NAKAI, S .
JOURNAL OF FOOD SCIENCE, 1974, 39 (01) :49-51
[3]   Thermal aggregation and gelation of soy globulin at neutral pH [J].
Chen, Nannan ;
Zhao, Mouming ;
Chassenieux, Christophe ;
Nicolai, Taco .
FOOD HYDROCOLLOIDS, 2016, 61 :740-746
[4]   Acid gelation of mixed thermal aggregates of pea globulins and β-lactoglobulin [J].
Chihi, Mohamed-Lazhar ;
Sok, Nicolas ;
Saurel, Remi .
FOOD HYDROCOLLOIDS, 2018, 85 :120-128
[5]   Molecular interactions and functionality of a cold-gelling soy protein isolate [J].
Cramp, G. L. ;
Kwanyuen, P. ;
Daubert, C. R. .
JOURNAL OF FOOD SCIENCE, 2008, 73 (01) :E16-E24
[6]  
EFTINK MR, 1991, METHOD BIOCHEM ANAL, V35, P127
[7]   Modulating fracture properties of mixed protein systems [J].
Ersch, Carsten ;
ter Laak, Irene ;
van der Linden, Erik ;
Venema, Paul ;
Martin, Anneke .
FOOD HYDROCOLLOIDS, 2015, 44 :59-65
[8]   Limited Aggregation Behavior of β-Conglycinin and Its Terminating Effect on Glycinin Aggregation during Heating at pH 7.0 [J].
Guo, Jian ;
Yang, Xiao-Quan ;
He, Xiu-Ting ;
Wu, Na-Na ;
Wang, Jin-Mei ;
Gu, Wei ;
Zhang, Yuan-Yuan .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2012, 60 (14) :3782-3791
[9]  
HASTINGS RJ, 1985, J FOOD SCI, V50, P503
[10]   STRUCTURE OF SOYA GLYCININ AND CONGLYCININ GELS [J].
HERMANSSON, AM .
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 1985, 36 (09) :822-832