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| 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 |
| Study on the influences of myoglobin on the gel properties of myofibrillar protein based on intermolecular forces and water migration |
| 投稿时间：2026-03-20 修订日期：2026-08-14 |
| DOI： |
| 中文关键词: 未漂洗鱼糜 肌红蛋白 肌原纤维蛋白 分子间作用力 水分分布迁移 |
| 英文关键词:unwashed surimi myoglobin myofibrillar protein molecular forces water migration |
| 基金项目:国家自然科学基金面上项目（32272256）、辽宁省自然基金面上项目“复热方式对鱼糜制品凝胶劣变与风味形成的作用机制研究”（编号2024010632-JH3/107）、辽宁省教育厅科学技术研究项目，多宝鱼预制菜加工及风味调控关键技术研究（项目编号LJ212410167068）,国家自然科学基金项目（面上项目，重点项目，重大项目） |
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| 中文摘要: |
| 目的 探究肌红蛋白在未漂洗鱼糜制品加工过程中对肌原纤维蛋白的凝胶劣化机制。方法 分析不同漂洗次数对白鲢鱼糜凝胶性能的影响，确认未漂洗鱼糜中肌红蛋白含量较高且凝胶性能较差；并以此构建肌红蛋白-肌原纤维蛋白混合体系，测定蛋白间疏水相互作用、氢键、离子键的变化，并利用低场核磁共振分析水分分布。结果 添加86 μmol/L肌红蛋白反应0 h后，疏水相互作用、氢键和离子键分别降低14.02%、19.86%和23.24%，反应24 h后各分子间作用力进一步减弱，凝胶网络变得粗糙松散；不易流动水（T23）峰面积占比下降3.84%，导致持水性降低、蒸煮损失增大。结论 肌红蛋白通过空间位阻干扰鱼糜蛋白间的分子交联，削弱分子间作用力，破坏凝胶网络结构，进而引发水分迁移与流失。本研究明确了肌红蛋白对肌原纤维蛋白凝胶网络的作用路径与影响规律，可为未漂洗鱼糜加工中通过调控内源性血红素蛋白来提升凝胶品质提供理论依据。 |
| 英文摘要: |
| Objective To investigate the mechanism by which myoglobin deteriorates the gelation properties of myofibrillar protein during the processing of unrinsed surimi products. Methods The effects of different rinsing cycles on the gel properties of silver carp surimi were analyzed to confirm that unrinsed 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 At 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. After 24 h of reaction, these intermolecular forces were further weakened, respectively, leading to a loose and coarse gel network. The proportion of immobilized water (T23) peak area decreased by 3.84% compared with the native myofibrillar protein control group, resulting in 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 have 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. |
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