Gel properties of surimi from silver carp (Hypophthalmichthys molitrix) as affected by heat treatment and soy protein isolate

Spray drying is used in the food industry to convert liquids into dry powders. The effect of the addition of salt ions before spray drying to improve the heat- and cold-induced gel properties of soy protein isolate (SPI) was investigated. Certain concentrations of Na+ (0.005–0.01 M), Mg2+ (0.005 M), and Ca2+ (0.005 M) significantly increased the hardness, springiness, cohesiveness, chewiness, gumminess, resilience, and water holding capacity of the heat- and cold-induced gels. This effect arises predominantly due to the functional groups buried in the protein matrix that are partially exposed to improve the interactions between the protein molecules. The main interactions that promoted gel formation and maintained the three-dimensional structure of the heat- and cold-induced gels were hydrophobic and disulfide interactions. Analysis using scanning electron microscopy showed that the heat- and cold-induced gels were uniform, had smooth surfaces, and had smaller pores with added Na+ (0.01 M), Mg2+ (0.005 M), and Ca2+ (0.005 M). The results indicate that we might broaden the applications of SPI by simulating the industrial gel manufacturing process for products such as fish balls and chiba tofu. Overall, adding salt ions before spray drying could offer great potential for the development of SPI with enhanced functionality suitable for comminuted meat products.

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Influence of Thermal Treatment and Soy Bean Protein Characteristics on Muscle Protein Emulsion Stability

Food Science and Technology International ◽

10.1177/1082013206065994 ◽

2006 ◽

Vol 12 (3) ◽

pp. 195-204 ◽

Cited By ~ 1

Author(s):

M. P. Rodríguez ◽

C. Regue ◽

A. Bonaldo ◽

C. Carrara ◽

L. G. Santiago

Keyword(s):

Heat Treatment ◽

Soy Protein ◽

Emulsion Stability ◽

Muscle Protein ◽

Soy Protein Isolate ◽

Protein Isolate ◽

Stable Emulsion ◽

Protein Isolates ◽

Interfacial Film ◽

Soy Protein Isolates

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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