Adenosine monophosphate boosts the cryoprotection of ultrasound-assisted freezing to frozen surimi: Insights into protein structures and gelling behaviors

Zhu, Xiangwei; He, Diheng; Chen, Yingying; Duan, Xinyu; Li, Yonghui; Yuan, Yue; Zhan, Fuchao; Li, Bin; Teng, Yongxin

doi:10.1016/j.foodchem.2024.139343

Food Chemistry

2024

DOI: 10.1016/j.foodchem.2024.139343

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Adenosine monophosphate boosts the cryoprotection of ultrasound-assisted freezing to frozen surimi: Insights into protein structures and gelling behaviors

Xiangwei Zhu,

Diheng He,

Yingying Chen

et al.

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2024

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Cited by 3 publications

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Co-stabilization effects of gluten/carrageenan to the over-heated myofibrillar protein: Inhibit the undesirable gel weakening and protein over-aggregations

Zhu,

Liu,

Ouyang

et al. 2024

International Journal of Biological Macromolecules

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Co-stabilization effects of gluten/carrageenan to the over-heated myofibrillar protein: Inhibit the undesirable gel weakening and protein over-aggregations

Zhu,

Liu,

Ouyang

et al. 2024

International Journal of Biological Macromolecules

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A comprehensive unraveling of the mystery of reduced-salt surimi gels: From molecular mechanism to future prospects

Li,

Chen,

You

et al. 2024

Trends in Food Science & Technology

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Soy Protein Isolate Gel Subjected to Freezing Treatment: Influence of Methylcellulose and Sodium Hexametaphosphate on Gel Stability, Texture and Structure

Xia,

Zhang,

Huang

et al. 2024

Foods

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Freezing affects texture and induces the loss of gel quality. This study investigated the effects of methylcellulose (MC) (0.2%, 0.4%, 0.6%) and sodium hexametaphosphate (SHMP) (0.15%, 0.3%) on the gel textural and structural properties of SPI gels before and after freezing, and explores the synergistic enhancement of gel texture and the underlying mechanisms resulting from the simultaneous addition of SHMP and MC to SPI gels. It was revealed that MC improved the strength of SPI gels through its thickening properties, but it could not inhibit the reduction of SPI gels after freezing. The 0.4% MC-SPI gel exhibited the best gel strength (193.2 ± 2.4 g). SHMP inhibited gel reduction during freezing through hydrogen bonding and ionic interactions; it enhanced the freezing stability of SPI gels. The addition of 0.15% SHMP made the water-holding capacity in SPI gels reach the highest score after freezing (58.2 ± 0.32%). The synergistic effect of MC and SHMP could improve the strength and the freezing stability of SPI gels. MC facilitated the release of ionizable groups within SPI, causing negatively charged SHMP groups to aggregate on the SPI and inhibit the freezing aggregation of proteins. These results provide a strong basis for the improvement of cryogenic soy protein gel performance by SHMP and MC.

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Adenosine monophosphate boosts the cryoprotection of ultrasound-assisted freezing to frozen surimi: Insights into protein structures and gelling behaviors

Cited by 3 publications

References 36 publications

Co-stabilization effects of gluten/carrageenan to the over-heated myofibrillar protein: Inhibit the undesirable gel weakening and protein over-aggregations

Co-stabilization effects of gluten/carrageenan to the over-heated myofibrillar protein: Inhibit the undesirable gel weakening and protein over-aggregations

A comprehensive unraveling of the mystery of reduced-salt surimi gels: From molecular mechanism to future prospects

Soy Protein Isolate Gel Subjected to Freezing Treatment: Influence of Methylcellulose and Sodium Hexametaphosphate on Gel Stability, Texture and Structure

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