Functional properties of soy protein isolates as affected by heat treatment during isoelectric precipitation

The effects of heat treatment on the interaction of salt soluble muscle protein and soy protein isolate in model emulsions were studied. Three soy protein isolates (SPI) were used: a commercial one (CSPI) and two pilot plant samples: a native soy protein isolate (NSPI) and an acid treated soy protein isolate (ASPI). Emulsions were prepared with muscle protein (MP), NSPI, ASPI, CSPI and mixtures of MP and the different SPIs, and then treated at 20, 55, 70, 80 and 90°C. Coalescence, soluble protein and electrophoresis of the aqueous phase of the emulsions were evaluated for each temperature. At 20°C the more native soy protein (NSPI) was compatible with MP, producing a stable emulsion that became more stable during heat treatment. CSPI alone could not form a stable interfacial film through the temperature range, however emulsion stabilisation was achieved at 55°C and 70°C when adding MP. Emulsions prepared with MP ASPI were highly unstable at 20°C, while as the emulsion temperature increased, coalescence decreased abruptly and maintained low values at every temperature. MP, NSPI, ASPI and MP NSPI produced stable emulsions both at 20°C and higher temperatures.

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EFFECTS OF DRYING METHOD ON PHYSICOCHEMICAL AND FUNCTIONAL PROPERTIES OF SOY PROTEIN ISOLATES

Journal of Food Processing and Preservation ◽

10.1111/j.1745-4549.2008.00357.x ◽

2009 ◽

Vol 34 (3) ◽

pp. 520-540 ◽

Cited By ~ 25

Author(s):

XIAO-ZHONG HU ◽

YONG-QIANG CHENG ◽

JUN-FENG FAN ◽

ZHAN-HUI LU ◽

KOHJI YAMAKI ◽

...

Keyword(s):

Functional Properties ◽

Soy Protein ◽

Drying Method ◽

Protein Isolates ◽

Soy Protein Isolates ◽

Physicochemical And Functional Properties

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Relationship between the Method of Obtention and the Structural and Functional Properties of Soy Protein Isolates. 2. Surface Properties. [Erratum to document cited in CA121:203670]

Journal of Agricultural and Food Chemistry ◽

10.1021/jf00051a057 ◽

1995 ◽

Vol 43 (3) ◽

pp. 854-854

Author(s):

S. Petruccelli ◽

M. C. Anon

Keyword(s):

Surface Properties ◽

Functional Properties ◽

Soy Protein ◽

Protein Isolates ◽

Soy Protein Isolates ◽

Structural And Functional Properties

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Characterizing the Structural and Functional Properties of Soybean Protein Extracted from Full-Fat Soybean Flakes after Low-Temperature Dry Extrusion

Molecules ◽

10.3390/molecules23123265 ◽

2018 ◽

Vol 23 (12) ◽

pp. 3265 ◽

Cited By ~ 3

Author(s):

Wenjun Ma ◽

Fengying Xie ◽

Shuang Zhang ◽

Huan Wang ◽

Miao Hu ◽

...

Keyword(s):

Functional Properties ◽

Soy Protein ◽

Activity Index ◽

Soybean Protein ◽

Stability Index ◽

Extrusion Temperature ◽

Emulsifying Activity ◽

Protein Isolates ◽

Soy Protein Isolates ◽

Structural And Functional Properties

The soy protein isolates (SPI) extracted from different extruded full-fat soybean flakes (FFSF), and their conformational and functional properties were characterized. Overall, the free thiol (SH) content of SPI increased when the extrusion temperature was below 80 °C and decreased at higher temperatures. Soy glycinin (11S) showed higher stability than β-conglycinin (7S) during extrusion. Results also indicated that the increase in some hydrophobic groups was due to the movement of hydrophobic groups from the interior to the surface of the SPI molecules at extrusion temperatures from 60 to 80 °C. However, the aggregation of SPI molecules occurred at extrusion temperatures of 90 and 100 °C, with decreasing levels of hydrophobic groups. The extrusion temperature negatively affected the emulsifying activity index (EAI); on the other side, it positively affected the emulsifying stability index (ESI), compared to unextruded SPI.

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