Thermal aggregation and gelation of soy globulin at neutral pH

被引：51

作者：

Chen, Nannan ^{[1
,2
]}

Zhao, Mouming ^{[1
]}

Chassenieux, Christophe ^{[2
]}

Nicolai, Taco ^{[2
]}

机构：

[1] South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Guangdong, Peoples R China

[2] LUNAM Univ Maine, IMMM UMR CNRS 6283, Polymeres Colloides & Interfaces, F-72085 Le Mans 9, France

来源：

FOOD HYDROCOLLOIDS | 2016年 / 61卷

关键词：

Soy globulin; Aggregate; Kinetics; Light scattering; Gel; SPI; LIGHT-SCATTERING; SOYBEAN PROTEINS; BETA-CONGLYCININ; WHEY PROTEINS; HEAT; DENATURATION; GELS; KINETICS; ISOLATE;

D O I：

10.1016/j.foodhyd.2016.06.028

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Aggregation of soy globulin was studied in salt free aqueous solution at neutral pH over a wide range of concentrations (0.3-90 g/L) and temperatures (50-95 degrees C). The structure of the aggregates that were formed during heating was characterized with light scattering. In all cases aggregates with the same self-similar structure were observed that were characterized by a fractal dimension d(f) = 2.0. Dynamic light scattering showed that the aggregates were flexible. The aggregate size increased with heating time and the rate of growth was characterized by an Arrhenius temperature dependence up to 85 degrees C with E-a = 180 kJ/mol independent of the concentration. For a given temperature the aggregation rate increased very strongly with increasing concentration. Gels were formed at concentrations down to 50 g/L and at temperatures down to 50 degrees C. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：740 / 746

页数：7

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