肌原纤维蛋白热诱导凝胶特性及化学作用力研究进展

肌原纤维蛋白是肉类食品中的主要蛋白质。在肉制品加工过程中,由于加热而形成的肌原纤维蛋白凝胶结构,决定着糜类肉制品的感官性质(如弹性、多汁性、黏性等)。蛋白质凝胶的形成是蛋白分子之间二硫键、氢键、疏水相互作用和静电相互作用的结果,而蛋白质的凝胶特性正是由这些作用力决定的。该文从肌原纤维蛋白热诱导凝胶形成机制、凝胶特性和凝胶化学作用力三方面总结了国内外肌原纤维蛋白凝胶特性(质构、保水、流变)和凝胶化学作用力研究现状,进而探讨了肌原纤维蛋白凝胶形成的深层次原因(作用力),为肉类凝胶制品的应用提供了理论依据。     

芸豆蛋白淀粉样纤维聚集后属性的变化研究

研究探讨了芸豆蛋白的淀粉样纤维聚集后的溶液和形成凝胶属性的变化.一定浓度的蛋白质溶液在低pH和低离子强度的条件下,加热可以形成线性聚集.蛋白质分子热聚集,导致了溶液和形成的凝胶性质上发生了较大的改变.淀粉样纤维蛋白质的形成可以通过刚果红的波长扫描来确定,流变仪测定蛋白溶液的粘度和形成凝胶的强度,扫描电镜观察蛋白质构象变化后的微观形态.     

大豆7S球蛋白凝胶光学性质的研究

本文深入地研究了大豆7S球蛋白凝胶光学和流变学性质与蛋白质浓度、加热温度和加热时间的关系。结果表明在形成蛋白质凝胶(蛋白质浓度≥7.5%)的前提下,低的蛋白质浓度有利于大豆7S球蛋白形成透明性凝胶,但凝胶强度较低;温度＞85℃有利于蛋白凝胶透明性和强度的提高;加热60min.较为适宜。扫描电子显微镜(SEM)观察显示大豆7S球蛋白透明凝胶具有有序微观结构;探讨了大豆7S球蛋白形成透明凝胶机理。可为进一步研究大豆蛋白凝胶的光学性质和研制透明的大豆蛋白产品提供理论依据。     

大豆11S和7S蛋白质凝胶特性的研究综述

按照大豆蛋白质的构成,可以把11S和7S蛋白质凝胶特性的研究相对划分为3种类型:①蛋白质组分类型,研究11S和7S蛋白质热致凝胶的形成条件和部分特性;②分离蛋白类型,研究以11S和7S蛋白质为主要成分的大豆分离蛋白(SPI)凝胶特性;③蛋白质亚基类型,研究11S和7S蛋白质亚基的结构与凝胶形成机理的关系。对3种类型的研究具有相对的先后顺序,即在蛋白质组分类型基础上进行SPI类型的研究,在组分和SPI类型基础上进行亚基类型的初步研究,今后将对蛋白质亚基类型做深入研究。     

酪蛋白与乳清蛋白比例对酸奶凝胶性质的影响

研究了乳中酪蛋白和乳清蛋白比例对凝固型酸奶流变学特性和微观结构的影响,结果表明,固定蛋白质质量分数、降低酪蛋白和乳清蛋白的比例,可以明显提高酸奶凝胶的质量.乳中蛋白质质量分数一致时,酸奶凝胶的硬度、黏度、持水力随着酪蛋白和乳清蛋白比例的减小而增大,凝胶网络结构变得更规则、致密,孔隙更小.在低蛋白质质量分数下,降低乳中酪...     

酸法脱酰胺大米蛋白/葡聚糖体系微结构性质研究

研究了酸法脱酰胺大米蛋白(ADRP)/葡聚糖混合体系的微观结构及流变性质。采用共聚焦激光扫描显微镜观察了ADRP/葡聚糖混合体系的微观结构,结果显示出ADRP之间产生了有效的交联,并且在蛋白质质量分数较高的混合体系中形成了蛋白质网状结构。流变仪观察了混合体系的动力学性质,黏度-剪切速率曲线表明蛋白质交联程度较高的体系黏度增加明显,频率扫描结果进一步证实蛋白质质量分数较高的体系凝胶网络结构的形成;质构仪测试了此凝胶体系的强度,证实混合体系凝胶比单一ADRP的蛋白凝胶具有更高的破裂强度。ADRP和葡聚糖的相分离是混合体系中蛋白质网络结构形成的可能原因。     

EGCG修饰对乳清蛋白乳液冷凝胶特性的影响

研究不同浓度表没食子儿茶素没食子酸酯(EGCG;2.7,13.3,26.6μmol多酚/g蛋白质)对乳清蛋白乳液冷凝胶微观结构及凝胶特性的影响.采用动态光散射和凯氏定氮法测定乳液的粒径、带电性质和界面蛋白吸附量,激光共聚焦显微镜观察乳液微观结构,分析EGCG对蛋白乳液微观结构和特性的影响.采用质构仪单轴压缩法测定凝胶强...     

温度及酶量对MTGase催化聚合WPC质构特性的影响

以乳清浓缩蛋白(WPC)为底物,探讨了不同的温度及酶量微生物转谷氨酰胺酶(MTGase)催化聚合WPC对其质构特性的影响.结果表明:MTGase催化聚合WPC,在有还原剂DTT存在的条件下,酶/蛋白质比为10U/g左右时,25～45 ℃的反应温度范围内,可以获得质构特性较好的凝胶.酶/蛋白质比及温度过低或过高,都不利于蛋白凝胶的形成.     

不同糖类对草鱼鱼糜凝胶的影响

研究葡聚糖,蔗糖,海藻糖,低聚木糖,低聚果糖对草鱼鱼糜凝胶微观结构、蛋白质结构、水分子分布及质构特性的影响.扫描电镜结果表明,与空白样相比,添加4％葡聚糖、蔗糖和海藻糖的鱼糜凝胶中能观察到更紧密的网络结构,糖的加入促进了蛋白质的交联和凝胶网络结构的紧密性,改善了鱼糜制品的凝胶特性.添加低聚果糖的样品使鱼糜蛋白α-螺旋结...     

四种常见豆类蛋白特性的研究

本文研究了绿豆、红豆、黄豆及芸豆四种常见豆类蛋白质的特性。使用差示扫描量热仪、流变仪和质构仪测定这些豆类蛋白在热变性过程中以及形成凝胶后的性质变化。结果表明不同蛋白质具有较大的性质差异,豆类蛋白质凝胶硬度大小顺序为:芸豆绿豆大豆红豆。使用原子力显微镜观察蛋白质加热前后的微观形态变化,与加热前相比,加热后豆类蛋白形成明显的热聚集,分子之间形成紧密连接。     

Rational Design of Amyloid‐Like Fibrillary Structures for Tailoring Food Protein Techno‐Functionality and Their Potential Health Implications

To control and enhance protein functionality is a major challenge for food scientists. In this context, research on food protein fibril formation, especially amyloid fibril formation, holds much promise. We here first provide a concise overview of conditions, which affect amyloid formation in food proteins. Particular attention is directed towards amyloid core regions because these sequences promote ordered aggregation. Better understanding of this process will be key to tailor the fibril formation process. Especially seeding, that is, adding preformed protein fibrils to protein solutions to accelerate fibril formation holds promise to tailor aggregation and fibril techno‐functionality. Some studies have already indicated that food protein fibrillation indeed improves their techno‐functionality. However, much more research is necessary to establish whether protein fibrils are useful in complex food systems and whether and to what extent they resist food processing unit operations. In this review the effect of amyloid formation on gelation, interfacial properties, foaming, and emulsification is discussed. Despite their prevalent role as functional structures, amyloids also receive a lot of attention due to their association with protein deposition diseases, prompting us to thoroughly investigate the potential health impact of amyloid‐like aggregates in food. A literature review on the effect of the different stages of the human digestive process on amyloid toxicity leads us to conclude that food‐derived amyloid fibrils (even those with potential pathogenic properties) very likely have minimal impact on human health. Nevertheless, prior to wide‐spread application of the technology, it is highly advisable to further verify the lack of toxicity of food‐derived amyloid fibrils.     

蛋白质凝胶机理的研究进展

凝胶特性是食品蛋白质的重要功能特性,蛋白质的凝胶行为及其流变性质是形成某些食品独特的质构、感官和风味的决定性因素。长期以来,人们对蛋白质的凝胶行为进行了广泛深入的研究,但对蛋白质凝胶的机理和凝胶动力学还没有完全了解。本文对当前有关蛋白质凝胶的类型、凝胶过程中蛋白质分子构象的变化、形成蛋白质凝胶的主要作用力和凝胶动力学过程的研究进展作了综述。随着现代分析研究技术的进步,对蛋白质凝胶行为的认识也逐渐深入。     

Physical effects upon whey protein aggregation for nano-coating production

Production of edible nanostructures constitutes a major challenge in food nanotechnology, and has attracted a great deal of interest from several research fields — including (but not limited to) food packaging. Furthermore, whey proteins are increasingly used as nutritional and functional ingredients owing to their important biological, physical and chemical functionalities. Besides their technological and functional characteristics, whey proteins are generally recognized as safe (GRAS). Denaturation and aggregation kinetics behavior of such proteins are of particular relevance toward manufacture of novel nanostructures possessing a number of potential uses. When these processes are properly engineered and controlled, whey proteins may form nanostructures useful as carriers of bioactive compounds (e.g. antimicrobials, antioxidants and nutraceuticals). This review discusses the latest advances in nano-scale phenomena involved in protein thermal aggregation aiming at formation of bio-based nano-coating networks. The extent of aggregation is dependent upon a balance between molecular interactions and environmental factors; therefore, the impact of these conditions is addressed in a critical manner. A particular emphasis is given to the effect of temperature as long as being one of the most critical variables. The application of moderate electric fields (MEF), an emergent approach, as such or combined with conventional heating is considered as it may inhibit/prevent excessive denaturation and aggregation of whey proteins — thus opening new perspectives for development of innovative protein nanostructures (i.e. nano-coatings). A better understanding of the mechanism(s) involved in whey protein denaturation and aggregation is crucial as it conveys information relevant to select methods for manipulating interactions between molecules, and thus control their functional properties in tailor-made applications in the food industry.     

植物蛋白凝胶及其应用研究进展

对近年来有关植物蛋白的凝胶机理、影响因素进行了综述,在此基础上,阐述了植物蛋白凝胶在食品领域及非食品领域的应用,提出了目前存在的研究空白及问题,为深入研究植物蛋白材料的应用及其降解机制、扩充植物蛋白的应用领域提供一些理论参考。     

Functional Characteristics of Milk Protein Concentrates and Their Modification

A major deterrent to the usage of milk protein concentrate (MPC), a high-protein milk product with increasing demand as a food and sports drink ingredient, has been its poor functional characteristics when compared with other milk protein products such as whey protein concentrate and sodium caseinates. This review discusses the recent research on functional properties of MPC, focusing on factors that may contribute to the poor functional characteristics before, during, and after production. Current research, methods employed, and new understanding on the causes of poor solubility of MPC at mild temperatures (about 20°C) has been presented, including loss of solubility during storage as these areas have received unprecedented attention over the past decade, and also affects other useful functional properties of MPC, such as emulsifying properties, gelation, and foaming. Processing methods, which include heat treatment, high-pressure application, microwave heating, ultrasound application, and enzyme and salts modification, have been used or have potential to modify or improve the functional properties of MPCs. Future research on the effects of these processing methods on the functional properties, including effects of enzyme hydrolysis on bitterness and bioactivity, has also been discussed.     

Nature of Stem Bromelain Treatments on the Aggregation and Gelation of Soybean Proteins

Aggregation and gelation of heated soybean proteins treated with stem bromelain were investigated by determination of sulfhydryl and hydrophobicity, by polyacrylamide gel electrophoresis and by scanning electron microscopy. The heat-induced, water-soluble soybean protein aggregates were initially unfolded by treatment with stem bromelain and released 7S and 4S proteins. The 2S protein was completely decomposed. The enzyme attacked the basic subunits of 11S globulin and converted them to low molecular weight fragments. Aggregation and gelation developed with icnrease of fragments. Noncovalent forces, possibly through hydrophobic interaction, played an important role in the aggregation process. Scanning electron microscopy revealed a fine network structure which suggested the combination of low molecular weight fragments.     

Influence of Cosolvent Systems on the Gelation Mechanism of Globular Protein: Thermodynamic,Kinetic, and Structural Aspects of Globular Protein Gelation

How thermostability and gelation of globular protein are affected by cosolvent systems present in food systems is critical to understanding their functionality. The expression of these functional attributes depends on the molecular structure and thermal‐mechanical history of the protein, as well as its chemical environment. To improve the design of processing protein‐containing food systems, one must fully understand the thermodynamic, kinetic, and structural impact of cosolvent on globular protein gelation. This review focuses on the impact of weakly interacting neutral cosolvent systems (for example, sugars and polyols) on the gelation of globular proteins. The physicochemical mechanisms by which these cosolvent systems can modulate protein gelation are highlighted from a thermodynamic, kinetic, and structural point of view.     

Properties of milk protein gels formed by phosphates

We investigated the properties of gels that were formed by adding emulsifying salts, such as tetrasodium pyrophosphate (TSPP), to reconstituted milk protein concentrate solution. The pH of a 51 g/L milk protein concentrate solution was adjusted to 5.8 after adding TSPP. Milk protein concentrate solutions were placed in glass jars and allowed to stand at 25°C for 24 h. Gels with the highest breaking force were formed when TSPP was added at a concentration of 6.7 mM, whereas no gel was formed when TSPP was added at concentrations of ≤2.9 or ≥10.5 mM. Several other phosphate-based emulsifying salts were tested but for these emulsifying salts, gelation only occurred after several days or at greater gelation temperatures. No gelation was observed for trisodium citrate. Gelation induced by TSPP was dependent on pH, and the breaking force of gel was greatest at pH 6.0. Furthermore, when the concentration of milk protein concentrate in solution was increased to 103 g/L, the breaking force of the gel increased, and a clearly defined network between caseins could be observed by using confocal scanning laser microscopy. These results suggest that TSPP-induced gelation occurs when the added TSPP acts with calcium as a cross-linking agent between dispersed caseins and when the balance between (a reduced) electrostatic repulsion and (enhanced) attractive (hydrophobic) interactions becomes suitable for aggregation and eventual gelation of casein molecules.     

Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation

Mechanical and structural properties of transglutaminase-induced casein gels are described here and compared with those of traditional acid casein gels. These gels were characterised by rheology and microscopy (confocal laser scanning microscopy and transmission electron microscopy). Unlike traditional casein gels produced by acidification and/or renneting which lead to gels cross-linked by weak physical interactions, gels formed using transglutaminase are covalently cross-linked. Gels with different characteristics can therefore be formed in this way and have some unusual and interesting features in terms of strength, kinetics of gelation, sensitivity to heat treatment and syneresis behaviour. The first steps of the transglutaminase-induced micellar aggregation were followed by turbidimetry and a mechanism for the aggregation process proposed.     

Improvement of canola protein gelation properties through enzymatic modification with transglutaminase

Enzymatic modification with transglutaminase (TG) was used to enhance the gelation of canola protein isolate (CPI) and thus improve its potential as a food ingredient. The effects of CPI concentration, TG concentration, treatment temperature and treatment time on CPI gelation properties were evaluated. A texture analyzer, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and scanning electron microscopy were used to characterize the resulting networks. The protein concentration, amount of TG, and treatment temperature were found to significantly impact gel strength. It was found that gelation can be improved by increasing the amounts of protein and TG and by keeping the treatment temperature close to 40 °C. SDS-PAGE showed that cross-linking of subunits occurred through TG treatment thus helping to explain the increase in gel strength observed during texture analysis. Micrographs further corroborated the trends noted during rheological studies.