Thermal stability and gel quality of myofibrillar protein as affected by soy protein isolates subjected to an acidic pH and mild heating

Niu, Haili; Xia, Xiufang; Wang, Chao; Kong, Baohua; Liu, Qian

doi:10.1016/j.foodchem.2017.09.055

Cited by 92 publications

(49 citation statements)

References 28 publications

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“…The literature identifies many factors that affect the gel properties of soy protein isolate, e.g., protein concentration, drying methods (spray drying, freeze drying, and vacuum drying), and environmental factors (pH, temperature, time, and salt ions) [5][6][7][8]. Spray drying has been shown to be a simple, low-cost, reproducible process.…”

Section: Introductionmentioning

confidence: 99%

Addition of Salt Ions before Spraying Improves Heat- and Cold-Induced Gel Properties of Soy Protein Isolate (SPI)

Teng

Wang

et al. 2019

Applied Sciences

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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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Section: Introductionmentioning

confidence: 99%

Addition of Salt Ions before Spraying Improves Heat- and Cold-Induced Gel Properties of Soy Protein Isolate (SPI)

Teng

Wang

et al. 2019

Applied Sciences

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“…However, little information is available concerning the application of BSDF on the gel quality of meat proteins in model system. Recent researches have paid much attention to the interaction between exogenous additives such as non-meat proteins, flaxseed gum, and fibres, with SSP or myofibrillar proteins for improving the quality of protein gels Liu et al, 2018;Niu, Xia, Wang, Kong, & Liu, 2018;Zhao, Zhou, & Zhang, 2019). However, few studies described the thermal stability and structural changes of dietary fibres-meat proteins composite gels, especially the addition of BSDF.…”

Section: Introductionmentioning

confidence: 99%

Effect of bamboo shoot dietary fiber on gel quality, thermal stability and secondary structure changes of pork salt-soluble proteins

Liu

Bai

et al. 2019

CyTA - Journal of Food

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2019) Effect of bamboo shoot dietary fiber on gel quality, thermal stability and secondary structure changes of pork salt-soluble proteins, ABSTRACTThe effect of bamboo shoot dietary fibre (BSDF) (0%-4%) on the gel quality, protein thermal stability and secondary structure of pork salt-soluble proteins (SSP) was investigated. The water holding capacity (WHC), breaking force and particle size were increased with the addition of 2% BSDF. Differential scanning calorimetry (DSC) analysis indicated that the addition BSDF changed the thermal denaturation temperature of myosin tail and actin, and led to the disappearance of myosin head as the increase of BSDF up to 4%. SDS-PAGE showed that the band intensity of actin was obviously enhanced by the addition of BSDF. Fourier transform infrared (FTIR) spectroscopy showed that BSDF could affect the protein secondary structure. The α-helix content was significantly decreased and the β-sheet content was significantly increased (P<0.05). In conclusion, BSDF could improve gel quality of salt soluble proteins and has a potential to be applied in meat products.

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“…The molecular forces involved in the gel network were dependent upon pH (Shimada & Cheftel, ; Li et al ., ; Niu et al ., ), salts (Li et al ., ), protein composition (Wu et al ., ) and thermal treatment conditions, such as heating time (Berghout et al ., ) and temperature (Wang et al ., ). Electrostatic interactions between proteins in gel network closely related to the pH and ionic strength of the system (Cavallieri et al ., ).…”

Section: Introductionmentioning

confidence: 99%

The relationship between breaking force and hydrophobic interactions or disulfide bonds involved in heat‐induced soy protein gels as affected by heating time and temperature

Hua

2018

Int J of Food Sci Tech

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Hydrophobic interactions and disulfide bonds involved in heat-induced soy protein gels were characterised by determining the dissolution kinetics of gels. Reducing SDS-PAGE results revealed that all proteins in gel network could be dissolved simultaneously by 1% (w/v) SDS solution, while a majority of glycinin (11S) A polypeptide and a moderate amount of 11S-B polypeptides, 7S-a 0 , a, c, and b subunits were found in 2% (w/v) DTT dissolving samples. Stronger interaction force between proteins in gel network would result in lower dissolution constant rate. The breaking force of soy gels increased from 543 to 2171 g force with increasing heating temperature from 85 to 100°C, and denaturation of 11S globulins played an important role in the development of gel network. As increasing heating time from 30 to 120 min, the breaking force of gels increased from 1687 to 2175 g force , then decreased to 1253 g force when the time was prolonged to 240 min. Negative correlations were observed between breaking force and dissolution constant rate k SDS or Dk, which suggested that the strengthening of both hydrophobic interactions and disulfide bonds.

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Thermal stability and gel quality of myofibrillar protein as affected by soy protein isolates subjected to an acidic pH and mild heating

Cited by 92 publications

References 28 publications

Addition of Salt Ions before Spraying Improves Heat- and Cold-Induced Gel Properties of Soy Protein Isolate (SPI)

Addition of Salt Ions before Spraying Improves Heat- and Cold-Induced Gel Properties of Soy Protein Isolate (SPI)

Effect of bamboo shoot dietary fiber on gel quality, thermal stability and secondary structure changes of pork salt-soluble proteins

The relationship between breaking force and hydrophobic interactions or disulfide bonds involved in heat‐induced soy protein gels as affected by heating time and temperature

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