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Study on the influences of myoglobin on the gel properties of myofibrillar protein based on intermolecular forces and water migration
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Bo-Yu ZHANG, Bo-Jun GUAN, Mu-Lin CHEN, Shu-Min YI*, Xue-Peng LI, Jian-Rong LI
Journal of Food Safety & Quality | 2026, 17(16) : 171 - 181
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Journal of Food Safety & Quality | 2026, 17(16): 171-181
• Special Topic: Processing and Quality Safety of Aquatic Products •
Study on the influences of myoglobin on the gel properties of myofibrillar protein based on intermolecular forces and water migration
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Bo-Yu ZHANG, Bo-Jun GUAN, Mu-Lin CHEN, Shu-Min YI*, Xue-Peng LI, Jian-Rong LI
Affiliations
  • College of Food Science and Engineering, Bohai University, Jinzhou 121013, China
doi: 10.19812/j.cnki.jfsq11-5956/ts.20260209006
Outline
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Objective

To investigate the mechanism by which myoglobin deteriorates the gelation properties of myofibrillar protein during the processing of unwashed surimi products.

Methods

The effects of different rinsing cycles on the gel properties of Hypophthalmichthys molitrix surimi were analyzed to confirm that unwashed surimi contains a higher level of myoglobin and exhibits poorer gel performance. A myoglobin‑myofibrillar protein mixed system was then constructed. Changes in hydrophobic interactions, hydrogen bonds and ionic bonds between proteins were measured, and water distribution was analyzed using low‑field nuclear magnetic resonance.

Results

After 0 h of reaction with 86 μmol/L myoglobin, hydrophobic interactions, hydrogen bonds and ionic bonds decreased by 14.02%, 19.86% and 23.24%, respectively, and the proportion of immobilized water (T23) peak area decreased by 3.84%. After 24 h of reaction, the deterioration intensified: all intermolecular forces further decreased compared with those at 0 h, and the T23 peak area proportion dropped to 87.90%, a decrease of 4.17% compared with the blank control group (0 μmol/L myoglobin) at the same time point. The gel network changed from dense and uniform to rough and loose, resulting in significantly reduced water‑holding capacity and increased cooking loss.

Conclusion

Myoglobin interferes with molecular cross‑linking between surimi proteins through steric hindrance, weakens intermolecular forces, disrupts the gel network structure, and consequently induces water migration and loss. This research has clarified the action path and influence rule of myoglobin on myofibrillar protein gel network, which can provide theoretical basis for improving the quality of gel by regulating endogenous heme protein during the processing of unwashed surimi gel.

unwashed surimi  /  myoglobin  /  myofibrillar protein  /  intermolecular forces  /  water migration
张博宇, 关博骏, 陈木林, 仪淑敏, 励建荣, 李学鹏. 基于分子间作用力与水分迁移的肌红蛋白对肌原纤维蛋白凝胶性能影响研究. 食品安全质量检测学报, 2026 , 17 (16) : 171 -181 . DOI: 10.19812/j.cnki.jfsq11-5956/ts.20260209006
Bo-Yu ZHANG, Bo-Jun GUAN, Mu-Lin CHEN, Shu-Min YI, Xue-Peng LI, Jian-Rong LI. Study on the influences of myoglobin on the gel properties of myofibrillar protein based on intermolecular forces and water migration[J]. Journal of Food Safety & Quality, 2026 , 17 (16) : 171 -181 . DOI: 10.19812/j.cnki.jfsq11-5956/ts.20260209006
Year 2026 volume 17 Issue 16
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doi: 10.19812/j.cnki.jfsq11-5956/ts.20260209006
  • Receive Date:2026-02-09
  • Online Date:2026-11-05
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  • Received:2026-02-09
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    College of Food Science and Engineering, Bohai University, Jinzhou 121013, China
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表12种不同金属材料的力学参数
科
Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)
属
Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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