物理法改善鱼肉蛋白功能特性研究概述

鱼肉是优质蛋白的重要来源。为了提高鱼肉蛋白的利用率,可通过物理方法改善蛋白质的功能特性,提升鱼肉蛋白的应用价值和应用前景。该文综述了几种改善鱼肉蛋白功能特性的物理新方法,阐述其对鱼肉蛋白功能特性的影响,并对物理法在鱼肉蛋白改性上深入研究进行展望,以期为鱼肉蛋白改性加工提供指导。     

糖基化反应改善蛋白质功能特性的研究进展

糖基化反应是改善蛋白质功能特性的一种有效的方法。主要介绍蛋白质糖基化反应机理,糖基化反应对鱼肉蛋白、β-乳球蛋白、卵清蛋白、酪蛋白、精蛋白以及酶等各类蛋白质功能特性影响的国内外研究进展。     

鱼肉蛋白质冷冻变性及抗冻剂的研究进展

本文简要分析了鱼肉蛋白冷冻变性的原因,主要综述了国内外鱼肉蛋白质冷冻变性的研究现状,并对糖类、盐类、乳蛋白、酶解产物等几种抗冻剂的应用作了详细介绍。展望了进一步研究鱼肉蛋白冷冻变性的新方向。     

酸碱处理对鱼肉蛋白凝胶特性影响的研究进展

我国鱼肉产量巨大,消费量也持续快速增长,但目前国内鱼肉精深加工技术落后,资源浪费严重。与传统加工处理相比,酸碱处理作为一种新型的肌肉蛋白提取和加工技术,不仅能提高蛋白回收率,还能改变蛋白构象,改善蛋白加工特性,提高产品附加值。本文概述酸碱处理对热诱导的鱼肉蛋白凝胶的强度、颜色和保水性等加工特性的影响,探讨了经过酸碱处理后肌球蛋白构象的变化,展望了酸碱处理在鱼肉精深加工领域的应用前景,为鱼肉制品品质改善和新产品研发提供科学依据。     

加热过程中肉嫩度变化的研究

肉在加热处理过程中嫩度发生了显著的变化。肉的剪切力值总体上呈现出先升后降的趋势,在0～100℃剪切力值不断上升,随着温度继续升高剪切力值开始下降,同时蒸煮损失随温度的升高而不断增加。导致这些变化的原因是加热过程中肉蛋白的热变性,其中肌原纤维蛋白和结缔组织蛋白的热变性是影响肉嫩度变化的主要因素。     

土耳其科学家研究用红外辅助欧姆加热预烹调肉丸的颜色、质构和烹调特性

正烹调肉制品的物理性质和品质严重受到加工温度和时间等热处理因素的影响,由热加工引起的蛋白变性会导致肉蛋白的紧缩,这样会产生大量的质量损失。随着科技的发展,相较于传统加热方式,欧姆和红外组合加热能够在促进产品品质提升的情况下,减小烹调时间。为研究应用红外加热辅助欧姆加热预烹调对肉丸品质特性的促进作用,土耳其科学家进行实     

不同质量比鸡胸肉、鸡腿肉混合肌原纤维蛋白的热诱导凝胶特性

以鸡胸肉和鸡腿肉为材料,研究鸡胸、鸡腿肉混合肌原纤维蛋白不同质量比(9:1、3:1、1:1、1:3、1:9)热变性温度、质构特性、流变特性和保水性的差异。结果表明：鸡胸肉肌原纤维蛋白的凝胶特性显著优于鸡腿肉,鸡胸肉与鸡腿肉的混合可以显著提升鸡腿肉蛋白的硬度、保水性;混合蛋白中,m鸡胸肉蛋白:m鸡腿肉蛋白为9:1的蛋白硬度、保水性最大,分别达到167.64g和83.6%,其凝胶特性和纯鸡胸肉差异不大;m鸡胸肉蛋白:m鸡腿肉蛋白为1:9的混合蛋白硬度、保水性和贮能模量终值均为最小,分别为110.82g、48.75%和297Pa,其凝胶特性优于纯鸡腿肉肌原纤维蛋白。     

辐照对肌肉蛋白结构及其凝胶性能影响的研究进展

对肉类食品来说,辐照不仅能有效杀灭其中的微生物,而且能作用于蛋白质等生物大分子,影响蛋白间的相互作用力,从而改变蛋白质构象,导致蛋白变性、聚集或凝胶化,因此利用电子束辐照处理,有望成为改善肌肉蛋白凝胶品质的一种有效手段。本文列举了常用于表征蛋白质结构的光学仪器如拉曼光谱、红外光谱、圆二色谱等在肌肉蛋白构象研究中的应用,综述了辐照引起肌肉蛋白生化特性、化学作用力和构象的改变,以及这种改变对肌肉凝胶网络结构形成的作用,在分子水平上探讨了辐照对肌肉凝胶特性的影响机理,为利用辐照技术改善肌肉凝胶性能提供理论指导。     

蛋白溶解性分析法研究大米焙炒过程中蛋白质热变性行为

考察了焙炒过程中大米蛋白质的热变性行为,通过大米蛋白在不同功能溶剂中的溶解度变化了解大米蛋白质在焙炒过程中次级结构的变化及热变性信息。发现热变性主要发生在焙炒的前期,热变性包括蛋白质次级结构的变化和更高能级的化学变化。与传统蒸煮方法相比,焙炒大米的蛋白质热变性程度较低。粳米和糯米中的蛋白质热变性行为基本相似,选用不同的加热介质对大米蛋白的热变性没有影响。     

鱼肉蛋白贮藏期间构象变化对功能特性的影响

蛋白质不仅是食品中的重要成分,其功能特性也是其它食品成分所不能比拟或代替的。蛋白质的功能性质决定了食品的结构、形态、色、香、味等。了解其功能特性,不仅有助于在食品加工业中正确使用蛋白质,也利于食品营养成分的保持和利用,因此蛋白质的研究与应用日益引起人们的关注。蛋白质的功能性质不仅取决于蛋白质的分子组成和结构特征,同时受环境因素和加工条件的影响。文章对鱼肉蛋白在贮藏期间构象的变化对其功能特性的影响进行了综述。     

Effect of heat treatment on milk protein functionality at emulsion interfaces. A review

Heat treatment affects the molecular structure of milk proteins at the interfaces of oil-in-water emulsions and in aqueous media. Experimental evidence of the impact of thermal processing on milk protein structure is presented and the contribution of whey proteins and caseins at film formation during emulsification is discussed. Recent advances in understanding the effect of heat treatment in milk protein functionality at emulsion interfaces are reviewed with particular emphasis on the emulsifying ability of whey proteins with or without the presence of the casein fraction. The major findings regarding the destabilizing mechanisms of oil-in-water emulsions brought about by heat-induced denaturation of milk proteins are presented. This paper aims to combine recent knowledge on how thermal processing of milk proteins affects their molecular configurations in bulk and particularly at interfaces, which in turn appear to be important with respect to the physico-chemical properties of milk protein-stabilized emulsions.     

乳清蛋白及与其它乳成分的热聚合作用机制研究进展

乳蛋白决定奶类品质,而热加工会影响乳清蛋白尤其是β-乳球蛋白的稳定性。热处理时,乳清蛋白不仅自身发生不同程度的聚合,而且通过巯基-二硫键分别与酪蛋白胶束和乳脂球膜蛋白发生结合。乳清蛋白亦可与其它乳成分如乳糖、钙盐、乳脂发生热聚合作用。本文根据乳品受热温度的不同,针对乳清蛋白间及其与其它乳成分的相互作用途径进行分析,阐明热聚合作用过程及机理,对改善乳制品的热稳定性、凝胶性等功能性质具有重要的理论意义,拓宽乳清蛋白作为配料在相关食品体系中的应用。     

Stability of Whey Proteins during Thermal Processing: A Review

Whey proteins have many benefits due to their high nutritional value and their various applications in food products. A drawback of whey proteins is their instability to thermal processing, which leads to their denaturation, aggregation, and, under some conditions, gelation. As thermal processing is a major treatment in the processing of milk and milk products, its influence on whey proteins has been extensively studied. Understanding the mechanisms involved during each stage of denaturation and aggregation of whey proteins is critical to devising ways of improving their stability. These aspects are reviewed in this paper. Also covered are approaches to preventing or reducing heat‐induced aggregation of whey proteins. Inhibition of aggregate formation has considerable potential for alleviating the problems that arise from the instability of whey proteins.     

Differential Scanning Calorimetry of Fish Muscle: The Effect of Processing and Species Variation

Differential Scanning Calorimetry (DSC) has been used to study the thermal properties of fish muscle proteins and to measure the extent of their denaturation under various processing conditions. Fish myosin was susceptible to denaturation by frozen storage and dehydration. Denaturation of certain fish proteins was partially reversible. Although fish myosin was very unstable, its thermal stability was found to increase in species adapted, to higher environmental temperatures.     

Thermal denaturation and functional properties of egg proteins in the presence of hydrocolloid gums

The aim of this study was to investigate the thermal stability, foaming and emulsifying properties of egg white and egg yolk constituents (egg yolk plasma and egg yolk granule) in the presence of hydrocolloid gums. Differential scanning calorimetry was used to examine the thermal stability of proteins. Heat denaturation of proteins were not influenced from the presence of anionic pectin and i-carrageenan and neutral guar gum. The residual denaturation enthalpy was observed to decrease as a result of protein aggregation. Thermal treatment have been observed to be detrimental to foaming capacity of egg white, while foam stability was improved. The foam stability was enhanced in the presence of pectin which may provide a strong viscoelastic film together with protein. Emulsifying activity and stability and of egg yolk granule and plasma were reduced after heat treatment. The presence of guar gum improved the emulsifying properties, while both pectin and guar gum reduced the rate and extend of creaming of egg yolk protein – stabilized proteins after heat treatment.     

热处理对肉类蛋白特性及有害物质产生的影响研究进展

肉类是人类获取重要蛋白质的主要来源,而热处理是肉类食用前不可或缺的加工环节。在热处理过程中,一系列的生化反应基本从改变肉蛋白质的特性开始,不同的热处理技术在赋予肉类显著风味的同时也会引起蛋白质特性发生显著改变。在三维结构上,热处理后肉类蛋白可以变性并形成聚集体。在分子水平上,热处理改变了蛋白质的一级结构,影响了包括蛋白质羰基化、芳香残基的修饰和美拉德反应产物的形成。此外,热处理还会引起大量有害物的形成。因此,探究热处理后肉类蛋白特性及有害物产生是确定肉类加工机理和更好控制其产品营养和功能特性的关键。本文系统综述了肉类在经过不同热处理后的蛋白特性（变性、聚集和氧化）以及有害物质（杂环胺和多环芳烃）生成和减控的策略,以期为肉类加工企业、中央厨房以及家庭饮食中获得安全、健康的高质量肉类提供实用指南和理论基础。     

冷冻贮藏引起的鱼肉蛋白变性及物理化学特性的变化

冷冻贮藏是鱼类重要的贮藏方法,但不适当的冻藏和缓化会引起鱼肉肌原纤维蛋白的变性,造成鱼肉质量降低。鱼肉蛋白质变性主要和蛋白质的结构变化有关,包括空间结构的变化、溶解性的变化、Ca2+-ATPase活性变化、巯基和二硫键含量变化、表面疏水性变化及海水鱼中甲醛含量的变化,而结构的变化进一步影响蛋白质的功能特性。本文主要论述鱼肉蛋白质的冷冻变性机理,并对鱼肉蛋白质在冷冻贮藏期间引起的蛋白质物理化学特性的变化进行论述。     

Modifying the Functional Properties of Egg Proteins Using Novel Processing Techniques: A Review

Egg proteins can be used in a wide range of food products, owing to their excellent foaming, emulsifying, and gelling properties. Another important functional property is the susceptibility of egg proteins to enzymatic hydrolysis, as protein digestion is closely related to its nutritional value. These functional properties of egg proteins are likely to be changed during food processing. Conventional thermal processing can easily induce protein denaturation and aggregation and consequently reduce the functionality of egg proteins due to the presence of heat‐labile proteins. Accordingly, there is interest from the food industry in seeking novel nonthermal or low‐thermal techniques that sustain protein functionality. To understand how novel processing techniques, including high hydrostatic pressure, pulsed electric fields, ionizing radiation, ultraviolet light, pulsed light, ultrasound, ozone, and high pressure homogenization, affect protein functionality, this review introduces the mechanisms involved in protein structure modification and describes the structure–functionality relationships. Novel techniques differ in their mechanisms of protein structure modification and some have been shown to improve protein functionality for particular treatment conditions and product forms. Although there is considerable industrial potential for the use of novel techniques, further studies are required to make them a practical reality, as the processing of egg proteins often involves other influencing factors, such as different pH and the presence of other food additives (for example, salts, sugar, and polysaccharides).     

蛋白质热聚集行为机理及其对蛋白质功能特性影响的研究进展

蛋白质热聚集行为是食品加工过程中较常发生的现象。热处理条件会使蛋白质结构发生变化,引起蛋白质的理化性质的改变,从而导致蛋白质发生热聚集。热聚集体的大小、形态、界面性等直接影响蛋白质凝胶特性、溶解性、起泡性、乳化性等功能特性,从而影响富含蛋白质食品的品质。本文介绍了蛋白质热聚集行为的机理、分类和表征手段,重点综述了蛋白质热聚集行为的影响因素,及蛋白质热聚集行为对蛋白质功能特性的影响,为研究复杂蛋白质体系热聚集行为及对食品品质的影响提供理论基础。     

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.