Characteristics Comparative Study on Two Extraction Types of Soy Protein Isolates

Characteristics Comparative Study on Two Extraction Types of Soy Protein Isolates
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发表时间:
2006
期刊:
Food Science
影响因子:
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通讯作者:
Qiu Ai-yong
Qiu Ai-yong
中科院分区:
其他
文献类型:
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作者:
Qiu Ai-yong

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脱脂大豆片用含水乙醇洗涤,所得材料用水提取,以制备大豆分离蛋白(SPI-A),与直接从碱性低变性大豆片中提取的常规大豆分离蛋白(SPI-C)相比,其功能性质有所改善。在蛋白质浓度为12%(W/W)时,用流变仪测定了SPI-A的凝胶特性,其凝胶破裂力为385.4g,明显高于SPI-C的凝胶破裂力(85.4g)。通过醇洗还发现乳化和起泡稳定性得到改善。高效尺寸排阻色谱显示,当SPI-A和SPI-C在大约相同时间洗脱时,激光散射分析表明SPI-A溶液含有比SPI-C具有更大流体动力学半径的颗粒,表明SPI-A形成具有更柔性结构的更大蛋白质聚集体,而SPI-C形成更小且更紧凑的聚集体。
Defatted soy flakes were washed with aqueous alcohol and the resultant material was extracted with water to prepare soy protein isolate (SPI-A) with improved functional properties in comparing with the conventional soy protein isolate(SPI-C)extracted directly from the alkaline low-denatured soy flakes. Gelling property was determined by rheometer at the protein concentration of 12% (W/W) while the gel fracture force of SPI-A was 385.4g, substantially higher than that of SPI-C (85.4g). Emulsifying and foaming stability were also found to be improved through alcohol washing. High performance size exclusion chromatography showed that when SPI-A and SPI-C were both eluted around the same time, the laser light scattering analysis indicated that SPI-A solution contains particles with larger hydrodynamic radius than SPI-C, suggesting that SPI-A forms larger protein aggregates with more flexible structure whereas SPI-C forms smaller and more compacted aggregates.