The effects of calcium chloride on the gel properties of porcine myosin–κ-carrageenan mixtures

Pan, Teng; Guo, Huiyuan; Li, Yuan; Song, Junhong; Ren, Fazheng

doi:10.1016/j.foodhyd.2016.09.026

Cited by 83 publications

(22 citation statements)

References 66 publications

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“…The hardness of the cold-induced gel was decreased. These results might be due to the gel strength being related to the amount of protein involved in the formation of the network structure and the forces forming the network structure [23][24][25]. The addition of Na+ diminishes repulsive forces, and protein-protein association occurs, forming a self-supporting gel [26].…”

Section: Texture Properties Of the Gelsmentioning

confidence: 99%

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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: Texture Properties Of the Gelsmentioning

confidence: 99%

“…(a) Ions could enhance the interactions within the gel system when the ionic concentrations were from 0.005 to 0.01 M, and the hydrophobic interactions and disulfide bond interactions were the main interactions within the gels [23,46]. Heat-induced gels had stronger interactions than cold-induced gels.…”

Section: Chemical Interaction Forces Analysismentioning

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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“…The extraction of myosin was according to the literature ( Han et al, 2015 ; Pan et al., 2017 ) with some modifications. All steps of the extraction were taken at 4°C.…”

Section: Methodsmentioning

confidence: 99%

“…Centrifugation was used to analyze the WHC (%) based on the method developed by Pan et al (2017) with a slight modification. Each gel was centrifuged at 10,000×g for 10 min at room temperature.…”

Section: Water Holding Capacity Measurementmentioning

confidence: 99%

The Effect of Age on the Myosin Thermal Stability and Gel Quality of Beijing Duck Breast

Wei

Pan

Liu

et al. 2020

Food Sci Anim Resour

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The effect of age (22, 30, 38, and 46 days) on Beijing duck breast myosin gels was investigated. The results showed that the water holding capacity (WHC) and gel strength were markedly improved at the age of 30 days. Differential scanning calorimetry suggested that the myosin thermal ability increased at the age of 30 and 38 days (p<0.05). A compact myosin gel network with thin cross-linked strands and small regular cavities formed at the age of 30 days, which was resulted from the higher content of hydrophobic interactions and disulfide bonds. Moreover, the surface hydrophobicity of myosin extracted from a 30-day-old duck breast decreased significantly under temperature higher than 80℃ (p<0.05). This study illustrated that myosin extracted from a 30-day-old duck's breast enhanced and stabilized the WHC, thermal stability and molecular forces within the gel system. It concluded that age is an essential influencing factor on the myosin thermal stability and gel quality of Beijing duck due to the transformation of fibrils with different myosin character.

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“…The WHC of the MP gels was determined in accordance with the method of Pan et al . () with slight modification. In brief, 3 g of the gel samples was centrifuged (10 000 × g , 15 min, 4 °C), and the supernatant fluid was drained.…”

Section: Methodsmentioning

confidence: 99%

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

Wang

Gan

et al. 2018

Int J of Food Sci Tech

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Summary We investigated the effect of peroxyl radicals (ROO·), which are products of lipid peroxidation, on the structure and gel properties of myofibrillar proteins (MPs) isolated from rabbit meat. 2,2′‐Azobis(2‐amidinopropane) dihydrochloride (AAPH) was heated to stably derive ROO·. As the AAPH concentration increased, the protein carbonyl compounds significantly accumulated (P < 0.05), and the total sulfhydryl content was significantly lost (P < 0.05). Circular dichroism spectra, UV absorption spectra, intrinsic fluorescence spectra and surface hydrophobicity revealed that ROO· caused protein unfolding and conformational changes in MPs. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) analysis indicated that moderate (0–3 mm) and relatively high (5 and 10 mm) AAPH concentrations could lead to protein crosslinking and protein aggregation, respectively. These changes in protein structure could influence the gelling properties of MPs. Low‐level protein oxidation could increase gel strength and water holding capacity, whereas high‐level protein oxidation could reduce gel properties.

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The effects of calcium chloride on the gel properties of porcine myosin–κ-carrageenan mixtures

Cited by 83 publications

References 66 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)

The Effect of Age on the Myosin Thermal Stability and Gel Quality of Beijing Duck Breast

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

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