Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Xu, Yongxia; Wang, Rui; Zhao, Huanxin; Zhao, Jiamei; Li, Xuepeng; Shi, Yi Wei; Lǐ, Jiànróng; Sun, Xiaotao

doi:10.1002/jsfa.10130

Cited by 29 publications

(13 citation statements)

References 41 publications

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“…Non-reducing electrophoresis cannot disrupt the disulphide bonds. Therefore, it reflects the original composition of the various proteins in a mixed protein ( Figure 1 and Table 2 ), and both BL and Co contained myosin heavy chain (MHC, ~200 kDa), convicilin (~70 kDa), legumin (~62 kDa), vicilin (~50 kDa), actins (AC, ~42 kDa), legumin α (~38 kDa), tropomyosin (TM, ~34 kDa), and legumin β (~22 kDa), all aggregates consistent with the literature [ 25 , 26 ]. Compared with legumin α + β, vicilin is more flexible and exhibits higher interfacial activity [ 27 ].…”

Section: Resultssupporting

confidence: 86%

Effect of Pre-Emulsion of Pea-Grass Carp Co-Precipitation Dual Protein on the Gel Quality of Fish Sausage

Zhou

Zhang

Zhao

et al. 2022

Foods

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Currently, the processing method of introducing plant protein into meat products has attracted great attention. However, the direct addition of plant protein often leads to a decline in meat product quality. This paper aims to provide an efficient method for incorporating plant protein into fish sausage. Pea protein isolate (PPI), grass carp protein isolate (CPI) and pea-grass carp coprecipitated dual protein (Co) were derived from pea and grass carp by an isoelectric solubilisation/precipitation method. At the same time, the blended dual protein (BL) was obtained by blending PPI with CPI, and the plant and animal protein content of Co and BL was both controlled to be the same. The four proteins were combined with soybean oil and water to form a three-phase pre-emulsification system of protein-oil-water, which was added to grass carp meat as a replacement for animal fat to prepare fish sausage. The gelation properties of the four fish sausages and those without protein were analysed. The results showed that the gel quality of PPI fish sausage is poor, while the overall quality of Co fish sausage as a whole was significantly superior to that of PPI and BL, which was equivalent to CPI fish sausage. The sensory score of the Co fish sausage was slightly lower than that of CPI, but it had significantly higher water-holding capacity and hardness (p < 0.05). The Co fish sausage showed the synergistic effect of heterologous proteins, while BL had some antagonistic effects. This study shows that Co pre-emulsion is an effective strategy to introduce plant protein, so it has a good application prospect in the meat industry.

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Section: Resultssupporting

confidence: 86%

Effect of Pre-Emulsion of Pea-Grass Carp Co-Precipitation Dual Protein on the Gel Quality of Fish Sausage

Zhou

Zhang

Zhao

et al. 2022

Foods

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“…The protein compositions of BL and Co were analyzed via reducing and non-reducing SDS-PAGE. As can be seen in Figure 2 and Table 1 , both BL and Co contained myosin heavy chain (MHC, ~200 kDa), convicilin (~70 kDa), legumin (~62 kDa), vicilin (~50 kDa), actins (AC, ~42 kDa), legumin α (~38 kDa), tropomyosin (TM, ~34 kDa), legumin β (~22 kDa), and aggregates consistent with the literature [ 28 , 29 ]. To sum up, both BL and Co effectively combined pea and CPI, and thus, both are suitable for further testing.…”

Section: Resultssupporting

confidence: 88%

A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation

Zhou

Zhang

Cao

et al. 2021

Foods

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Currently, the application of protein mixture derived from plants and animals is of great interest to the food industry. However, the synergistic effects of isolated protein blends (BL) are not well established. Herein, the development of a more effective method (co-precipitation) for the production of protein mixtures from pea and grass carp is reported. Pea protein isolate (PPI), grass carp protein isolate (CPI), and pea–carp protein co-precipitates (Co) were prepared via isoelectric solubilization/precipitation using peas and grass carp as raw materials. Meanwhile, the BL was obtained by blending PPI with CPI. In addition, the subunit composition and functional properties of Co and BL were investigated. The results show that the ratios of vicilin to legumin α + β and the soluble aggregates of Co were 2.82- and 1.69-fold higher than that of BL. The surface hydrophobicity of Co was less than that of BL, PPI, and CPI (p < 0.05). The solubility of Co was greater than that of BL, PPI, and CPI (p < 0.05), and the foaming activity was higher than that of BL and CPI (p < 0.05) but slightly lower than that of PPI. In addition, based on the emulsifying activity index, particle size, microstructure, and viscosity, Co had better emulsifying properties than BL, PPI, and CPI. The study not only confirmed that co-precipitation was more effective than blending for the preparation of mixed protein using PPI and CPI but also provided a standard of reference for obtaining a mixture of plant and animal proteins.

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“…The binding capacity of natural myosin to several flavour compounds ranged between 18% and 28%. The binding ability of myosin to various aldehydes was positively correlated with the length of the carbon chain, which was consistent with existing studies (Xu et al ., 2019a; Lin et al ., 2020). Moreover, the adsorption capacity of 1‐octene‐3‐ol to myosin was weaker than that of aldehydes.…”

Section: Resultsmentioning

confidence: 99%

Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

Yin

et al. 2022

Int J of Food Sci Tech

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The effects of yeast β-glucan (YG) on the aggregation and flavour adsorption capacity of Spanish mackerel myosin under two-step heat treatments were investigated. The surface hydrophobicity and active sulfhydryl content of heat-induced myosin was increased by the addition of YG, reaching the maximum values of 81.46 and 17.49 mol per 10 5 g after heating at 90 °C for 10 min. YG incorporation significantly decreased the α-helix content of myosin to the minimum value of 48.27%, whereas the β-sheet was increased. The addition of YG promoted the unfolding of myosin, exposing more hydrophobic bonding sites, thus enhancing the flavour-binding capacity of myosin. Lengthy heating at 90 °C combined with YG addition accelerated the cross-linking and aggregation of myosin, leading to the re-embedding of the exposed hydrophobic groups as much as the reduction of flavour-binding sites. However, YG's unique porous structure could also boost the flavour adsorption ability of myosin containing YG.

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Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Cited by 29 publications

References 41 publications

Effect of Pre-Emulsion of Pea-Grass Carp Co-Precipitation Dual Protein on the Gel Quality of Fish Sausage

Effect of Pre-Emulsion of Pea-Grass Carp Co-Precipitation Dual Protein on the Gel Quality of Fish Sausage

A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation

Impacts of yeast β‐glucan on thermal aggregation and flavour adsorption capacity of Spanish mackerel myosin

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