Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating

Niu, Haili; Li, Yue; Han, Jung‐Soon; Liu, Qian; Kong, Baohua

doi:10.1016/j.foodhyd.2017.04.001

Cited by 68 publications

(31 citation statements)

References 33 publications

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“…Dynamic rheological properties were evaluated according to the procedure described by Niu, Li, Han, Liu, and Kong () with some modifications. The rheological properties of meat batters during the heating process were determined with a rheometer (DHR‐1, TA Instruments Inc., New Castle, DE, USA) equipped with two parallel plates (40 mm dia) set at 1 mm apart.…”

Section: Methodsmentioning

confidence: 99%

Enhancement of the Textural and Gel Properties of Frankfurters by Adding Thermo‐reversible or Thermo‐irreversible Curdlan Gels

Jiang

Cao

Xia

et al. 2019

Journal of Food Science

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The influence of different addition levels (0.1% to 0.5%) of thermo-reversible curdlan gels (TRC) and thermoirreversible curdlan gels (TIRC) on the physicochemical and textural characteristics of frankfurters, as well as dynamic rheological properties of meat batters, was investigated. Increased percentages of TRC and TIRC were associated with lower cooking loss and quicker relaxation times, as well as superior emulsion stability, and higher L * -values and b * -values of frankfurters (P < 0.05). Moreover, with equal curdlan concentrations from 0.3% to 0.5%, TRC showed higher hardness and chewiness values than those with added TIRC (P < 0.05), but the gumminess, springiness, and resilience values were almost the same between each treatment (P > 0.05). The textural profile results were in strong agreement with the rheological data. Principal component analysis revealed that certain quality attributes were affected differently by the inclusion levels of TRC and TIRC. Additionally, the distinctive mechanism of the formation of the complex meat protein network by TRC or TIRC was also clarified and verified via scanning electron microscopy analysis. Further studies will investigate the molecular interactions of meat proteins with these two types of curdlan gels as a function of addition levels.Practical Application: Curdlan can form two different types of gels mainly depending on heating temperature, designated as thermo-reversible curdlan gels (TRC) and thermo-irreversible curdlan gels (TIRC), respectively. The addition of these two gels could improve the textural and gel properties of frankfurters, as well as improve the rheological profiles of meat batters. Each gel type invokes a different mechanism of influence on the formation of the complex meat protein network. Results indicate that TRC (mainly as an effective gelling agent) and TIRC (mainly as a potential fat-mimetic) can provide distinctive frankfurter formulations catered to the requirements preferred by different consumers.

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Section: Methodsmentioning

confidence: 99%

Enhancement of the Textural and Gel Properties of Frankfurters by Adding Thermo‐reversible or Thermo‐irreversible Curdlan Gels

Jiang

Cao

Xia

et al. 2019

Journal of Food Science

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“…The surf clams are known for their delicate and sweet taste with a high content of myofibrillar protein (MP), a type of protein with important biological functions in the body. It is well-known that the MP plays a pivotal role in determining protein properties of food products, such as water holding capacity (WHC), production yield, and texture of sausage products [2][3][4]. Heating is usually involved in preparing MP products, and the thermal-induced gelation of MP leads to gel formation with high strength.…”

Section: Introductionmentioning

confidence: 99%

Assessment of Water Mobility in Surf Clam and Soy Protein System during Gelation Using LF-NMR Technique

Wang

Cheng

et al. 2020

Foods

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Water mobility and distribution of a dual-protein system of surf clam myofibrillar protein (MP) and soy protein (SP) was investigated by the nondestructive low field nuclear magnetic resonance (LF-NMR) technique. Four proton populations were found in the contour plots of T2 relaxation times for the SP-MP system. The first component, (T21), was assigned to the highly integrated water located in protein macromolecules with a relaxation time of approximately 1.15 ms. The second signal, T22, with a relaxation time of 2.20 to 38.00 ms was regarded as the inter-myofibrillar water trapped in organized protein structures. The third component, T23, with a relaxation time of around 100 ms was ascribed to the extra-myofibrillar water. With an increase in temperature, T24 appeared which was assigned to the free water within the extra-myofibrillar space. The gelation behavior occurred at 70, 62, and 52 °C as the proportion of SP/MP was 4:6, 2:8, and 0:10, respectively. The principal component analysis (PCA) and heatmap of LF-NMR data analysis showed potential for distinguishing the different dual-protein systems formed at various temperatures. The analysis of storage modulus G′, loss modulus G″, and tanδ confirmed the change trend of the LF-NMR results. The measurements of cooking loss, water holding capability, and gel strength further revealed that the SP and MP were likely to form a gel network with an increase of additional clam protein. The hydrophobicity analysis showed, for the systems with the SP/MP proportions of 4:6, 2:8, and 0:10, more hydrophobic groups were exposed when the temperature was over 50 °C. Scanning electron microscopy showed that the number of the micropores increased with an addition of MP in the dual-protein system of SP/MP. All the results demonstrated that LF-NMR has great potential for characterizing the gelation process of a dual-protein system.

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“…Soy protein isolate (SPI) is an important food ingredient and is often used in human foods due to its nutritional value and technological properties, as well as its relatively low price [1]. The gel properties are important functional properties of SPI.…”

Section: Introductionmentioning

confidence: 99%

“…Traditionally, SPI is added in the industrial production of emulsified muscle foods to improve product texture and yield [2,3]. However, this increases the cost because of the gel softening of natural soy protein isolate (N-SPI) with the extension of the storage period [1,4]. Furthermore, Wang et al (2015) reported that N-SPI had a negative effect on the gel properties of some meat proteins.…”

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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Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating

Cited by 68 publications

References 33 publications

Enhancement of the Textural and Gel Properties of Frankfurters by Adding Thermo‐reversible or Thermo‐irreversible Curdlan Gels

Enhancement of the Textural and Gel Properties of Frankfurters by Adding Thermo‐reversible or Thermo‐irreversible Curdlan Gels

Assessment of Water Mobility in Surf Clam and Soy Protein System during Gelation Using LF-NMR Technique

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

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