Minxin Lu , Chang Zhang , Linyin Ma , Shucheng Liu , Hui Teng , Lei Chen
{"title":"磁场辅助冷冻结合莪术对万年青肌纤维蛋白的低温保护作用:氧化聚集、蛋白质结构和热稳定性","authors":"Minxin Lu , Chang Zhang , Linyin Ma , Shucheng Liu , Hui Teng , Lei Chen","doi":"10.1016/j.foodhyd.2024.110730","DOIUrl":null,"url":null,"abstract":"<div><div>To counteract the negative effects of conventional freezing methods on frozen surimi products, the present study investigated the effects of magnetic field (MF) freezing in combination with different amounts of curdlan (CUR) on oxidative denaturation, structural alterations, and thermal stability of myofibrillar protein (MP) in shrimp surimi. The results indicated that the intervention of magnetic fields alone improved the quality of frozen muscle proteins. Under the dual intervention of magnetic field-assisted freezing and CUR, small ice crystals formed with MF6 treatment resulted in significantly lower solubility, turbidity, and mean particle size than the control group (<em>p</em> < 0.05). Moreover, the oxidation of MP was also significantly slowed down by inhibiting the formation of hydrophobic groups and carbonyl groups, maintaining a high content of sulfhydryl groups. MF6 also exhibited a high Ca<sup>2+</sup>-ATPase activity. The α-helix content, the increase in fluorescence intensity under this condition also tend to make the secondary and tertiary structures of myofibrillar protein more stable. Meanwhile, electrophoretic profiles and CLSM showed that this condition maintains the integrity of the MP. In addition, the MF6 samples also had high protein thermal stability. However, excess CUR reduces the excellence of MP cryoprotection. As a result, MF6 has better protection and improvement effects on protein function, structure and thermal stability, and CUR was also found to have the potential for cryoprotectant development.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110730"},"PeriodicalIF":11.0000,"publicationDate":"2024-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Cryoprotective effect of magnetic field-assisted freezing in combination with curdlan on myofibrillar protein of Litopenaeus vannamei: Oxidative aggregation, protein structure and thermal stability\",\"authors\":\"Minxin Lu , Chang Zhang , Linyin Ma , Shucheng Liu , Hui Teng , Lei Chen\",\"doi\":\"10.1016/j.foodhyd.2024.110730\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>To counteract the negative effects of conventional freezing methods on frozen surimi products, the present study investigated the effects of magnetic field (MF) freezing in combination with different amounts of curdlan (CUR) on oxidative denaturation, structural alterations, and thermal stability of myofibrillar protein (MP) in shrimp surimi. The results indicated that the intervention of magnetic fields alone improved the quality of frozen muscle proteins. Under the dual intervention of magnetic field-assisted freezing and CUR, small ice crystals formed with MF6 treatment resulted in significantly lower solubility, turbidity, and mean particle size than the control group (<em>p</em> < 0.05). Moreover, the oxidation of MP was also significantly slowed down by inhibiting the formation of hydrophobic groups and carbonyl groups, maintaining a high content of sulfhydryl groups. MF6 also exhibited a high Ca<sup>2+</sup>-ATPase activity. The α-helix content, the increase in fluorescence intensity under this condition also tend to make the secondary and tertiary structures of myofibrillar protein more stable. Meanwhile, electrophoretic profiles and CLSM showed that this condition maintains the integrity of the MP. In addition, the MF6 samples also had high protein thermal stability. However, excess CUR reduces the excellence of MP cryoprotection. As a result, MF6 has better protection and improvement effects on protein function, structure and thermal stability, and CUR was also found to have the potential for cryoprotectant development.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"160 \",\"pages\":\"Article 110730\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2024-10-10\",\"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/S0268005X2401004X\",\"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/S0268005X2401004X","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
为了抵消传统冷冻方法对冷冻鱼糜产品的负面影响,本研究调查了磁场(MF)冷冻与不同量的可得然(CUR)相结合对虾糜中肌纤维蛋白(MP)的氧化变性、结构改变和热稳定性的影响。结果表明,单独的磁场干预能提高冷冻肌肉蛋白质的质量。在磁场辅助冷冻和 CUR 的双重干预下,MF6 处理形成的小冰晶导致溶解度、浑浊度和平均粒径显著低于对照组(p <0.05)。此外,通过抑制疏水基团和羰基的形成,保持高含量的巯基,MP 的氧化速度也明显减慢。MF6 还表现出较高的 Ca2+-ATPase 活性。在此条件下,α-螺旋含量、荧光强度的增加也使肌原纤维蛋白质的二级和三级结构更加稳定。同时,电泳图谱和 CLSM 显示,这种条件保持了 MP 的完整性。此外,MF6 样品还具有较高的蛋白质热稳定性。然而,过量的 CUR 会降低 MP 低温保护的优异性。因此,MF6 对蛋白质的功能、结构和热稳定性具有更好的保护和改善作用,同时还发现 CUR 具有开发冷冻保护剂的潜力。
Cryoprotective effect of magnetic field-assisted freezing in combination with curdlan on myofibrillar protein of Litopenaeus vannamei: Oxidative aggregation, protein structure and thermal stability
To counteract the negative effects of conventional freezing methods on frozen surimi products, the present study investigated the effects of magnetic field (MF) freezing in combination with different amounts of curdlan (CUR) on oxidative denaturation, structural alterations, and thermal stability of myofibrillar protein (MP) in shrimp surimi. The results indicated that the intervention of magnetic fields alone improved the quality of frozen muscle proteins. Under the dual intervention of magnetic field-assisted freezing and CUR, small ice crystals formed with MF6 treatment resulted in significantly lower solubility, turbidity, and mean particle size than the control group (p < 0.05). Moreover, the oxidation of MP was also significantly slowed down by inhibiting the formation of hydrophobic groups and carbonyl groups, maintaining a high content of sulfhydryl groups. MF6 also exhibited a high Ca2+-ATPase activity. The α-helix content, the increase in fluorescence intensity under this condition also tend to make the secondary and tertiary structures of myofibrillar protein more stable. Meanwhile, electrophoretic profiles and CLSM showed that this condition maintains the integrity of the MP. In addition, the MF6 samples also had high protein thermal stability. However, excess CUR reduces the excellence of MP cryoprotection. As a result, MF6 has better protection and improvement effects on protein function, structure and thermal stability, and CUR was also found to have the potential for cryoprotectant development.
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.