肌原纤维蛋白凝胶形成机理及影响因素的研究进展

肌原纤维蛋白的凝胶特性是肉类制品重要的功能特性,是形成肉制品独特的质构、保水性、乳化性以及感官的决定性因素。本文介绍了蛋白质凝胶形成的机理,重点论述了肌原纤维蛋白形成良好凝胶的影响因素,为生产高质量的肉制品提供理论依据。     

蛋白添加剂增强肉制品凝胶性研究进展

凝胶性作为肉类食品的重要特性之一,是影响肉制品外观、风味、质构的重要因素,增强肉制品的凝胶性对于改善肉制品的工艺和品质具有重要意义。肉制品加工中蛋白质形成聚集体的含量、结构、聚集速率等都会影响肉制品的凝胶性,而蛋白质添加剂可在一定程度上替代肌原纤维蛋白的凝胶和乳化作用,优化产品的感官和营养特性,并降低成本,成为肉制品研发和工艺优化的研究热点。本文对肌原纤维蛋白凝胶形成机理的研究进行汇总,并综述目前主要蛋白添加剂的性质和应用,以及蛋白添加剂与多糖胶体、酶制剂、磷酸盐进行复配增强肉制品凝胶性的研究进展,为凝胶肉制品的提质增效提供参考。     

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。     

亲水胶体对肌原纤维蛋白凝胶特性的研究进展

肌原纤维蛋白在动物肌肉中含量丰富,是日常饮食中获得氨基酸的重要来源。肉制品的加工通常依赖肌原纤维蛋白优异的功能特性,因此肌原纤维蛋白是一类重要的蛋白质。亲水胶体是长链聚合物(多糖和蛋白质)的异质组,广泛用于许多食品配方中以改善质量属性和保质期。亲水胶体用途广泛,主要作为增稠剂和胶凝剂。肌原纤维蛋白的凝胶强度受到亲水胶体的种类和作用方式的影响。该综述阐明了肌原纤维蛋白凝胶的形成机理,亲水胶体对肌原纤维蛋白凝胶的作用机理以及亲水胶体在肌原纤维蛋白中的应用,为改善肌原纤维蛋白凝胶特性提供参考,并提出未来的研究方向。     

超高压对肌原纤维蛋白结构及其凝胶特性影响的研究进展

应用超高压技术不仅可以减少肉制品中的微生物数量,保持良好的风味和质量,而且可以通过影响胶原纤维蛋白中二硫键、氢键、疏水作用等化学作用力,引起蛋白质构象发生改变,导致蛋白质变性、凝胶化和解聚,从而改善肉制品的凝胶性能。文章综述了超高压处理对肌原纤维蛋白生化特性、化学作用力的影响,讨论了超高压对肌原纤维蛋白凝胶特性的影响机制,为超高压技术在凝胶类肉制品中的应用提供理论参考。     

植物多酚改善肌原纤维蛋白凝胶特性的研究进展

肌原纤维蛋白是肌肉中最主要的蛋白质,其凝胶特性决定了肉制品的感官品质。植物多酚因独特的结构,可在热诱导过程中与肌原纤维蛋白相互作用,改变蛋白的结构并促进蛋白的交联聚集,故影响蛋白的成胶过程与凝胶特性。本文综述植物多酚在正常离子强度下、低离子强度以及氧化体系下促进肌原纤维蛋白热诱导凝胶形成过程及其机理,旨在为以绿色方法改善凝胶肉制品品质提供新思路。     

复合肌原纤维蛋白的凝胶特性

温度是影响蛋白质凝胶特性的主要因素。实验通过研究复合肌原纤维蛋白凝胶(猪肉肌原纤维蛋白、鲢鱼肉肌原纤维蛋白质量比分别为2∶0、1∶1、0∶2)在70、80、90、100℃加热时色泽、凝胶强度、质构特性、水分分布的变化,对复合肌原纤维蛋白凝胶和单一肌原纤维蛋白凝胶之间凝胶特性的差异和相关性进行研究,优化蛋白凝胶加热温度。结果表明:1∶1复合的肌原纤维蛋白凝胶能结合单一蛋白凝胶的特点,改善肌原纤维蛋白的凝胶特性;低场核磁共振表明,温度可通过影响水分分布来影响蛋白质的凝胶特性;蛋白凝胶特性随温度升高而增强,但温度过高会出现劣化,90℃是较为理想的加热温度。     

肌原纤维蛋白对挥发性风味物质吸附作用研究进展

蛋白质对挥发性风味物质的吸附作用一定程度上决定着食品风味品质。肌原纤维蛋白功能特性的变化会直接影响其对肉制品主效风味成分的吸附能力,因此对肌原纤维蛋白功能特性的影响因素进行深入研究对明晰肌原纤维蛋白与挥发性风味物质相互作用机制具有重要意义。本文就肌原纤维蛋白对挥发性风味物质的吸附机制、影响因素、研究技术与方法进行综述,详细介绍肌原纤维蛋白、挥发性风味成分以及多种外界因素对肌原纤维蛋白与挥发性风味物质相互作用影响的研究现状,并对肌原纤维蛋白对挥发性风味物质吸附作用研究尚未深入发掘的领域进行展望,为探究肌原纤维蛋白风味吸附作用在肉制品加工领域的生产应用提供理论参考。     

小麦麸膳食纤维对猪肉肌原纤维蛋白凝胶功能特性的影响

为开发低脂肪多纤维的健康肉制品,明确膳食纤维添加对肉制品品质的影响,以猪肉肌原纤维蛋白为研究对象,利用单因素分析法研究肌原纤维蛋白热诱导凝胶性质及小麦麸膳食纤维对猪肉肌原纤维蛋白功能特性的影响。结果表明：肌原纤维蛋白变性聚集的温度范围是40～70 ℃;肌原纤维蛋白凝胶硬度和保水性随肌原纤维蛋白质量浓度增加而增大,当质量浓度到达70 mg/mL时,凝胶硬度和保水性趋于稳定;pH值为5.5时肌原纤维蛋白凝胶硬度达到最大,凝胶保水性在pH 7.0时趋于稳定;离子强度为0.6 mol/L时凝胶的硬度和保水性趋于稳定。随着小麦麸膳食纤维添加量的增加,肌原纤维蛋白乳化性有所升高但是不明显,当添加量为5%时,乳化性增加7.4%,肌原纤维蛋白乳化稳定性降低;蛋白的弹性模量增大;凝胶硬度和保水性提高,添加量为4%时变化趋于平缓。随着膳食纤维粒径的减小,肌原纤维蛋白凝胶硬度和保水性逐渐提高;微观结构更加致密;蛋白弹性模量降低。由此可见,膳食纤维能够明显改变肌原纤维蛋白功能特性,通过在肉制品中添加适量的膳食纤维可以明显改良肉制品的风味,并替代脂肪,减少人体热量的摄入。     

相互作用下多酚对肌原纤维蛋白结构和性质的影响研究进展

肌原纤维蛋白是肌肉中的一类非常重要的蛋白质,直接影响肉制品的品质,但肌原纤维蛋白在加工贮藏过程中又极易发生氧化,导致加工肉品的氨基酸侧链修饰、蛋白质交联聚集以及功能性质改变等一系列不良后果。多酚类化合物作为抗氧化效果显著的天然抗氧化剂,与肌原纤维蛋白相互作用可有效抑制其氧化反应,同时也会对其结构、功能和营养特性产生影响。本文综述了肌原纤维蛋白氧化的自由基链式反应机制、多酚的构效关系、多酚-肌原纤维蛋白共价和非共价相互作用的机制及其对蛋白结构和性质的影响,以期能为多酚在肉制品保藏中的应用提供理论指导。     

Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation

Texture of meat products is dependent on the gelation characteristics of myofibrillar protein. Gaining an understanding of the gelation mechanism of meat gel systems is beneficial for the development of processed meat products as well as maintaining quality in meat products. The aim of this study was to investigate the impact of pH (5.6, 6.0, 6.5, and 7.0) on heat-induced gelation properties of myofibrillar proteins from porcine semimembranosus muscle. Dynamic rheological measurements were taken as the temperature increased by 1°C/min from 20 to 85°C, followed by a holding phase at 85°C for 3min to ensure complete gelation and during a subsequent cooling where the temperature dropped from 85 to 5°C at a rate of 5°C/min. Storage modulus (G') increased as gel formation occurred, but decreased after reaching the temperature of myosin denaturation (52°C) until approximately 60°C when the gel strength increased again. This resulted in a peak and subsequent depression in the data. This depression in the curve was more pronounced with increasing pH. Results indicate protein denaturation and gel formation are pH dependent. Furthermore, rate of gelation appears to influence water-holding capacity.     

Combination of high pressure and heat on the gelation of chicken myofibrillar proteins

The effects of combinations of high pressure and heat on chicken myofibrillar gels were investigated. High pressure was either applied simultaneously with heating (heating under pressure, HUP), before heating (PBH) or no high pressure with heat-only (HT). PBH treatment induced many similar properties in gels as did by HT treatment, except that PBH treatment promoted secondary structure transformation and formed more covalent bonds. HUP treatment resulted in less heat denaturation of the protein, induced fewer hydrophobic interactions and covalent bonds, hindered secondary and tertiary structural transformation, and formed a gel with a more porous microstructure. The gels induced by HUP treatment had softer texture and higher water holding capacity than gels induced by PBH or HT treatments. These findings suggest that high pressure with HUP treatment changes gel properties by resisting the heat-induced denaturation and gelation of myofibrillar proteins, while high pressure with PBH treatment alters gel properties by promoting denaturation of myofibrillar proteins.Industrial relevanceThe main constituents in meat are myofibrillar proteins, which are responsible for the functional properties of processed meat products. The gelation of myofibrillar proteins differs according to the sequence in which pressure/temperature combinations are applied. The pressure-modified protein interactions should be considered when adopting high pressure in meat product processing since the microstructure of the meat gel is affected by pressure, which would further affect water holding capacity and textural properties. HUP treatment showed its advantages in forming a fine microstructure and improving water-holding capacity.     

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic–protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat-induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose-dependent and dual-role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross-linked three-dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.     

非肉蛋白对肌原纤维蛋白及肉品品质影响的研究进展

肌原纤维蛋白的乳化特性和凝胶特性对食品的质地、风味及感官特性都极为重要。非肉蛋白由于具有较高营养价值及价格低廉的优势,逐渐成为肉制品中外源添加物的更好选择。本文主要综述非肉蛋白的添加对肌原纤维蛋白乳化和凝胶体系稳定性的影响,进一步分析非肉蛋白对肉制品品质的影响,旨在为非肉蛋白改善肉制品品质提供理论指导,进而为非肉蛋白在食品中的应用提供理论参考。     

Effect of High Pressure on Physicochemical Properties of Meat

The application of high pressure offers some interesting opportunities in the processing of muscle-based food products. It is well known that high-pressure processing can prolong the shelf life of meat products in addition to chilling but the pressure-labile nature of protein systems limits the commercial range of applications. High pressure can affect the texture and gel-forming properties of myofibrillar proteins and, hence, has been suggested as a physical and additive-free alternative to tenderize and soften or restructure meat and fish products. However, the rate and magnitude at which pressure and temperature effects take place in muscles are variable and depend on a number of circumstances and conditions that are still not precisely known. This review provides an overview of the current knowledge of the effects of high pressure on muscle tissue over a range of temperatures as it relates to meat texture, microstructure, color, enzymes, lipid oxidation, and pressure-induced gelation of myofibrillar proteins.     

Effect of feed texture, meal frequency and pre-slaughter fasting on carcass and meat quality, and urinary cortisol in pigs

The gelation characteristics of myofibrillar proteins are indicative of meat product texture. Defining the performance of myofibrillar proteins during gelation is beneficial in maintaining quality and developing processed meat products and processes. This study investigates the impact of pH on viscoelastic properties of porcine myofibrillar proteins prepared from different muscles (semimembranosus (SM), longissimus dorsi (LD) and psoas major (PM)) during heat-induced gelation. Dynamic rheological properties were measured while heating at 1 °C/min from 20 to 85 °C, followed by a holding phase at 85 °C for 3 min and a cooling phase from 85 to 5 °C at a rate of 5 °C/min. Storage modulus (G′, the elastic response of the gelling material) increased as gel formation occurred, but decreased after reaching the temperature of myosin denaturation (52 °C) until approximately 60 °C when the gel strength increased again. This resulted in a peak and depression in the thermogram. Following 60 °C, the treatments maintained observed trends in gel strength, showing SM myofibrils produced the strongest gels. Myofibrillar protein from SM and PM formed stronger gels at pH 6.0 than at pH 6.5. Differences may be attributed to subtle variations in their protein profile related to muscle type or postmortem metabolism. Significant correlations were determined between G′ at 57, 72, 85 and 5 °C, indicating that changes affecting gel strength took effect prior to 57 °C. Muscle type was found to influence water-holding capacity to a greater degree than pH.     

碱性氨基酸调控肌原纤维蛋白加工性能及肉品品质研究进展

随着《“健康中国2030”规划纲要》的实施以及消费者健康饮食观念的不断增强,“低盐无磷”健康肉制品逐渐成为肉制品行业未来的发展趋势。但是单纯减少NaCl以及多聚磷酸盐的添加量会严重影响产品的得率和品质。因此,寻求NaCl以及多聚磷酸盐的绿色健康替代物具有重要意义。近年来,碱性氨基酸——精氨酸、赖氨酸及组氨酸在肉制品行业中作为NaCl以及多聚磷酸盐替代物的研究与应用受到了广泛关注。本文综述了国内外有关碱性氨基酸对肌原纤维蛋白结构、溶解度、乳化性及凝胶性的调控作用及其内在机制的最新研究成果,并概述了碱性氨基酸对肉品品质（色泽、保水性、质构特性、氧化稳定性）的作用机理,以期为碱性氨基酸在肉类工业中的后续研究和实际应用提供理论依据。     

Functionality of muscle constituents in the processing of comminuted meat products

Comminuted meat systems represent a complex matrix of constituent interactions where physical and chemical properties of constituents determine the ultimate stability of the product. The functionality of the myofibrillar proteins varies with extent of extractability, ionic, and pH conditions. Primary functional responses of water binding (protein‐water interaction), fat holding and emulsification (protein‐lipid interaction) and gelation (protein‐protein interaction) are also temperature dependent in the course of processing sequences encountered during comminution and heat processing. Basic concepts and results of applied studies have been critically reviewed to emphasize the interactive effects of the myofibrillar proteins as the predominant constituent controlling the extent of formation and behavior of the comminuted meat matrix.     

鸡胸肉肌原纤维蛋白的提取及凝胶特性的研究

研究从鸡胸肉中提取肌原纤维蛋白，探讨不同pH值对肌原纤维蛋白含量的影响。研究结果：在pH7．0时，蛋白含量最大为69．74％，通过SDS—PAGE凝胶电泳分析表明，其主要成分为肌球蛋白、肌动蛋白和肌动球蛋白及其他一些小分子肌原纤维蛋白碎片；在离子强度0．6、pH7．0时提取的肌原纤维蛋白所制备的凝胶的保水性、硬度、胶粘性最大。