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Characteristics Comparative Study on Two Extraction Types of Soy Protein Isolates

Qiu Ai-yong

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Abstract

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.

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What this paper is about

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.

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Available abstract

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.

Key concepts: Soy protein, Chemistry, Chromatography, Size-exclusion chromatography, Extraction (chemistry), Aqueous solution, Rheology, Materials science

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