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Physical and chemical properties of soy protein isolates treated with sodium sulphite under low temperature extrusion

文献类型： 外文期刊

作者： Su, Xiaofang 1 ; Li, Fang 1 ; Gong, Yanfei 1 ; Dai, Meiyao 1 ; Pan, Weichun 3 ; Zhang, Bo 1 ;

作者机构： 1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Key Lab Agroprod Proc, Minist Agr, Beijing 100193, Peoples R China

2.Hangzhou Niuquxing Biol Technol Co Ltd, Dept Res & Dev, Hangzhou 311234, Peoples R China

3.Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Hangzhou 310018, Peoples R China

关键词： Disulphide bonds; extrusion; physicochemical properties; sodium sulphite; soy protein isolate

期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：2.773； 五年影响因子：2.516 ）

ISSN： 0950-5423

年卷期：

页码：

收录情况： SCI

摘要： Soy protein isolates (SPIs) treated with sodium sulphite (Na2SO3) under low temperature (50 degrees C) extrusion were investigated to create a system where the disulphide bonds were destroyed. The physicochemical properties of the extrudates were characterised after the addition of 0.0%, 1.5% and 3.0% (w/w) Na2SO3. Under these conditions, free sulfhydryl content significantly increased (from 98.46 to 449.64 mu mol g(-1)), specific mechanical energy during extrusion significantly increased (from 426.91 to 593.39 kJ kg(-1)), degradation temperature reduced (from 315.7 to 302.0 degrees C), protein solubility of the water extraction increased incrementally (from 5.41% to 20.17%) and water absorption capacity decreased (from 3.51% to 2.69%). Moreover, the addition of Na2SO3 caused a blue shift in the tryptophan fluorescence spectra of soluble SPI. These results suggest that Na2SO3 breaks disulphide bonds in SPI, which accelerates protein molecule denaturation to promote peptide disentanglement; consequently, SPI become more hydrophobic and less thermally stable.

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