提高乳化肌原纤维蛋白凝胶的抗冻融性能:淀粉晶型和疏水修饰对双重结构调节的影响

IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED
Yuxin Ding , Zhiwen Shen , Yujie Ding , Yanshun Xu , Dawei Yu , Zhifei Zhu
{"title":"提高乳化肌原纤维蛋白凝胶的抗冻融性能:淀粉晶型和疏水修饰对双重结构调节的影响","authors":"Yuxin Ding ,&nbsp;Zhiwen Shen ,&nbsp;Yujie Ding ,&nbsp;Yanshun Xu ,&nbsp;Dawei Yu ,&nbsp;Zhifei Zhu","doi":"10.1016/j.foodhyd.2025.111727","DOIUrl":null,"url":null,"abstract":"<div><div>Freeze-thaw (FT) deterioration severely limits the functional stability of emulsified myofibrillar protein (MP) gels, primarily due to interfacial protein film (IPF) disruption and bulk network collapse caused by ice/lipid crystallization. This study elucidated the synergistic mechanism by which starch crystalline polymorphs (A-, B-, and C-types) combined with octenyl succinic anhydride (OSA) esterification enhanced the FT stability of emulsified MP gels. Among the natural starches, A-type starch outperformed B- and C-types by maintaining tight interfacial co-adsorption and double-network entanglement with MP, providing a structural basis for cryoprotection. Building on this, OSA-induced amphiphilic modification further reinforced gel stability. OSA-starch anchored the interfacial film through hydrophobic interactions and strengthened cross-linking with the hydrophilic bulk network, thereby preserving desirable gel properties under FT stress. This dual structural stabilization, resulting from the appropriate OSA distribution and hydrophilic-lipophilic balance in A-OS starch, effectively inhibited ice/lipid crystallization and maintained matrix continuity in the emulsified MP gel. Macroscopic assessments, texture analysis, and microscopic observations confirmed that A-OS imparted superior liquid retention (thawing loss: 0.61 %; cooking loss: 3.03 %) and mechanical properties (hardness: 1307.88 g; springiness: 93.65 %) to the frozen gels, significantly outperforming other starch formulations. This work provides novel insights into stabilization strategies for protein-lipid colloidal systems and promotes the industrial application of high-quality frozen foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111727"},"PeriodicalIF":11.0000,"publicationDate":"2025-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Improved freeze-thaw resistance of emulsified myofibrillar protein gels: Effects of starch crystalline polymorphs and hydrophobic modification on dual structural regulation\",\"authors\":\"Yuxin Ding ,&nbsp;Zhiwen Shen ,&nbsp;Yujie Ding ,&nbsp;Yanshun Xu ,&nbsp;Dawei Yu ,&nbsp;Zhifei Zhu\",\"doi\":\"10.1016/j.foodhyd.2025.111727\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Freeze-thaw (FT) deterioration severely limits the functional stability of emulsified myofibrillar protein (MP) gels, primarily due to interfacial protein film (IPF) disruption and bulk network collapse caused by ice/lipid crystallization. This study elucidated the synergistic mechanism by which starch crystalline polymorphs (A-, B-, and C-types) combined with octenyl succinic anhydride (OSA) esterification enhanced the FT stability of emulsified MP gels. Among the natural starches, A-type starch outperformed B- and C-types by maintaining tight interfacial co-adsorption and double-network entanglement with MP, providing a structural basis for cryoprotection. Building on this, OSA-induced amphiphilic modification further reinforced gel stability. OSA-starch anchored the interfacial film through hydrophobic interactions and strengthened cross-linking with the hydrophilic bulk network, thereby preserving desirable gel properties under FT stress. This dual structural stabilization, resulting from the appropriate OSA distribution and hydrophilic-lipophilic balance in A-OS starch, effectively inhibited ice/lipid crystallization and maintained matrix continuity in the emulsified MP gel. Macroscopic assessments, texture analysis, and microscopic observations confirmed that A-OS imparted superior liquid retention (thawing loss: 0.61 %; cooking loss: 3.03 %) and mechanical properties (hardness: 1307.88 g; springiness: 93.65 %) to the frozen gels, significantly outperforming other starch formulations. This work provides novel insights into stabilization strategies for protein-lipid colloidal systems and promotes the industrial application of high-quality frozen foods.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"170 \",\"pages\":\"Article 111727\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-07-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Hydrocolloids\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0268005X25006873\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X25006873","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0

摘要

冻融(FT)变质严重限制了乳化肌纤维蛋白(MP)凝胶的功能稳定性,主要是由于冰/脂质结晶引起的界面蛋白膜(IPF)破坏和大块网络崩溃。本研究阐明了淀粉晶体多晶(A型、B型和c型)与辛烯基丁二酸酐(OSA)酯化反应联合增强乳化MP凝胶FT稳定性的协同机制。在天然淀粉中,a型淀粉与MP保持紧密的界面共吸附和双网纠缠,优于B型和c型淀粉,为低温保护提供了结构基础。在此基础上,asa诱导的两亲性修饰进一步增强了凝胶的稳定性。osa -淀粉通过疏水相互作用锚定界面膜,并加强与亲水性体网络的交联,从而在FT应力下保持理想的凝胶性能。由于A-OS淀粉中适当的OSA分布和亲水-亲脂平衡,这种双重结构稳定有效地抑制了冰/脂的结晶,并保持了乳化MP凝胶中基质的连续性。宏观评估、结构分析和微观观察证实,A-OS具有优异的液体保留效果(解冻损失:0.61%;蒸煮损失:3.03%)和机械性能(硬度:1307.88 g;弹性:93.65%)的冷冻凝胶,显著优于其他淀粉配方。这项工作为蛋白质-脂质胶体系统的稳定策略提供了新的见解,并促进了高质量冷冻食品的工业应用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Improved freeze-thaw resistance of emulsified myofibrillar protein gels: Effects of starch crystalline polymorphs and hydrophobic modification on dual structural regulation

Improved freeze-thaw resistance of emulsified myofibrillar protein gels: Effects of starch crystalline polymorphs and hydrophobic modification on dual structural regulation
Freeze-thaw (FT) deterioration severely limits the functional stability of emulsified myofibrillar protein (MP) gels, primarily due to interfacial protein film (IPF) disruption and bulk network collapse caused by ice/lipid crystallization. This study elucidated the synergistic mechanism by which starch crystalline polymorphs (A-, B-, and C-types) combined with octenyl succinic anhydride (OSA) esterification enhanced the FT stability of emulsified MP gels. Among the natural starches, A-type starch outperformed B- and C-types by maintaining tight interfacial co-adsorption and double-network entanglement with MP, providing a structural basis for cryoprotection. Building on this, OSA-induced amphiphilic modification further reinforced gel stability. OSA-starch anchored the interfacial film through hydrophobic interactions and strengthened cross-linking with the hydrophilic bulk network, thereby preserving desirable gel properties under FT stress. This dual structural stabilization, resulting from the appropriate OSA distribution and hydrophilic-lipophilic balance in A-OS starch, effectively inhibited ice/lipid crystallization and maintained matrix continuity in the emulsified MP gel. Macroscopic assessments, texture analysis, and microscopic observations confirmed that A-OS imparted superior liquid retention (thawing loss: 0.61 %; cooking loss: 3.03 %) and mechanical properties (hardness: 1307.88 g; springiness: 93.65 %) to the frozen gels, significantly outperforming other starch formulations. This work provides novel insights into stabilization strategies for protein-lipid colloidal systems and promotes the industrial application of high-quality frozen foods.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Food Hydrocolloids
Food Hydrocolloids 工程技术-食品科技
CiteScore
19.90
自引率
14.00%
发文量
871
审稿时长
37 days
期刊介绍: Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication. The main areas of interest are: -Chemical and physicochemical characterisation Thermal properties including glass transitions and conformational changes- Rheological properties including viscosity, viscoelastic properties and gelation behaviour- The influence on organoleptic properties- Interfacial properties including stabilisation of dispersions, emulsions and foams- Film forming properties with application to edible films and active packaging- Encapsulation and controlled release of active compounds- The influence on health including their role as dietary fibre- Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes- New hydrocolloids and hydrocolloid sources of commercial potential. The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信