Changes in the myosin secondary structure and shrimp surimi gel strength induced by dense phase carbon dioxide

Guo, Minghui; Liu, Shucheng; Ismail, Marliya; Farid, Mohammed; Ji, Hongwu; Mao, Weijie; Gao, Jing; Li, Chengyong

doi:10.1016/j.foodchem.2017.01.050

Cited by 69 publications

(38 citation statements)

References 43 publications

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“…It was beneficial to the exposure of protein hydrophobic group, which could better interact with the starch and increase the gel strength and hardness of the surimi (Figure and Table ). The relevance of protein secondary structure and gel strength was in accordance with the previous study, in which it was found that the increase of gel strength in surimi was related to the increase of β‐sheet content (Guo et al, ). Moreover, Zhou et al () also reported that the hardness of surimi gels was negatively correlated to the α‐helix content and positively correlated to the β‐sheet content of surimi gels.…”

Section: Resultssupporting

confidence: 90%

The effect of modified starches on the gel properties and protein conformation of Nemipterus virgatus surimi

et al. 2019

Journal of Texture Studies

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The study investigated the effect of native cassava starch (NCS), hydroxypropylated starch, acetic acid esterification starch (AAES), acetylated distarch phosphate on gel properties and protein conformation of Nemipterus virgatus surimi. Addition of 10 g kg−1 NCS or 20 g kg−1 AAES could significantly promote the gel strength and textural profiles of the surimi gels (p < .05). The water holding ability and whiteness of surimi were remarkably increased when the four types of starch were added at all concentrations (p < .05). In rheological test, the lower G′ was observed in surimi samples added with starch at low temperature, suggesting starch played an inactive filler role in surimi. Along with the increase of starch additive amount, ionic bond and hydrophobic interaction first increased and then decreased, while hydrogen bond first decrease and then increased. According to Raman spectroscopy data, small content of starch promoted the heat‐induced conformational transition of surimi protein from α‐helix to β‐sheet, leading to the change in gel properties of surimi gels. Scanning electron microscopy photographs showed surimi gels added with 20 g kg−1 starch had the finer and denser network structure. Therefore, 20 g kg−1 AAES or 10 g kg−1 NCS or 10 g kg−1 HS could be proposed to a potential modifier to effectively improve the quality of surimi products.

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Section: Resultssupporting

confidence: 90%

The effect of modified starches on the gel properties and protein conformation of Nemipterus virgatus surimi

et al. 2019

Journal of Texture Studies

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“…It is well known that the secondary structure of a protein is the basis for its properties in a food system. During processing, the a-helix was shown to be negatively related to the elastic modulus of silver carp myosin and the gel strength of shrimp surimi, while the β-sheet was shown to be positively correlated [27,28]. It has been reported that the β-sheet and β-turn content in silver carp myosin increased after glycation, suggesting that a highly flexible conformation is important for determining its functional properties [29].…”

Section: Introductionmentioning

confidence: 99%

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

et al. 2019

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The secondary structure of a protein has been identified to be a crucial indicator that governs its water solubility. Tilapia protein isolate (TPI), soybean protein isolate (SPI), and tilapia-soybean protein co-precipitates (TSPC3:1, TSPC2:1, TSPC1:1, TSPC1:2, and TSPC1:3) were prepared by mixing tilapia meat and soybean meal at different mass ratios. The results demonstrated that the water solubility of TSPCs was significantly greater than that of TPI (p <0.05). The changes in ultraviolet–visible and near-ultraviolet circular dichroism spectra indicated that the local structure of TSPCs was different from that of TPI and SPI. Fourier transform infrared Spectroscopy revealed the co-existence of TPI and SPI structures in TSPCs. The secondary structures of TSPCs were predominantly α-helix and β-sheet. TSPC1:1 was unique compared to the other TSPCs. In addition, there was a good correlation between the water solubility and secondary structure of TSPCs, in which the correlation coefficients of α-helix and β-sheet were −0.964 (p <0.01) and 0.743, respectively. TSPCs displayed lower α-helix contents and higher β-sheet contents compared to TPI, which resulted in a significant increase in their water solubility. Our findings could provide insight into the structure–function relationship of food proteins, thus creating more opportunities to develop innovative applications for mixed proteins.

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“…Shrimp [8] and crab [9] allergens are among the major types of food allergens reported by the Food and Agriculture Organization (FAO). Both crustaceans have tropomyosin [10], arginine kinase [11, 12], myosin [13, 14], and sarcoplasmic calcium-binding protein allergens [15, 16]. The incidence of crustacean allergy is very common with 38% in food allergy [17].…”

Section: Introductionmentioning

confidence: 99%

Bifidobacterium lactisAmeliorates the Risk of Food Allergy in Chinese Children by Affecting Relative Percentage of Treg and Th17 Cells

Liu

Wei

Wang

2018

Canadian Journal of Infectious Diseases and Medical Microbiolog

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We aimed to explore the therapeutic effect of Bifidobacterium lactis on food allergy by investigating the percentage of Treg and Th17 cells in Chinese children and related molecular mechanisms. A total of 256 children with food allergy were evenly assigned into two groups: BG, the children received 10 ml B. lactis (1 × 106/ml) daily, and CG, the children received the solution without B. lactis daily for three months. Allergic symptoms, serum IgE, and food antigen-specific IgE were measured. A mouse allergy model was established by using shrimp tropomyosin and treated with B. lactis. Relative mRNA levels of Treg- and Th17-associated cytokines were measured by using quantitative PCR. The percentage of Treg and Th17 cells in spleen were measured by using flow cytometry. After 3-month therapy, the allergic symptoms of the BG were remarkably reduced when compared with the CG (P < 0.05). Serum levels of IgE and food antigen-specific IgE were decreased too (P < 0.05). Similar results were also found in a mouse allergy model. After B. lactis treatment, the relative mRNA level of FoxP3 was significantly enhanced in the B. lactis therapy group when compared to positive controls. In addition, relative mRNA levels of FoxP3 and TGF-β associated with Treg cells were increased, whereas relative mRNA levels of IL-17A and IL-23 associated with Th17 were reduced. B. lactis treatment significantly increased the ratio of Treg and Th17 cells in a mouse allergy model (P < 0.05). B. lactis effectively alleviates allergic symptoms by increasing the ratio of Treg and Th17 cells.

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Changes in the myosin secondary structure and shrimp surimi gel strength induced by dense phase carbon dioxide

Cited by 69 publications

References 43 publications

The effect of modified starches on the gel properties and protein conformation of Nemipterus virgatus surimi

The effect of modified starches on the gel properties and protein conformation of Nemipterus virgatus surimi

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

Bifidobacterium lactisAmeliorates the Risk of Food Allergy in Chinese Children by Affecting Relative Percentage of Treg and Th17 Cells

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