蛋白-多糖共价复合作用研究进展

介绍了蛋白-多糖共价复合作用模式,复合物对蛋白质乳 化性能、热稳定性、抗氧化性能以及抗菌性能等的影响以 及近年来国外在该领域的最新研究动态。作为新型的高 分子食品配料,蛋白质与多糖复合物的研制和应用必将 有着良好的前景。     

蛋白质-多糖复合物研究进展

蛋白质与多糖是食品中两类重要的营养成分,也是影响食品功能性的重要生物大分子。蛋白质-多糖复合反应是一种利用多糖改善蛋白功能性的有效方法。人类根据实际生产生活中的需要,有针对性地将二者进行复合,发现蛋白质-多糖复合物比其前体物质具有更良好的功能性;因此,蛋白质-多糖复合物逐渐成为研究热点。主要介绍蛋白质与多糖分子之间的结合方式、蛋白质-多糖复合物制备方法、制备蛋白质-多糖复合物的影响因素及蛋白质-多糖复合物在食品领域的应用现状。     

蛋白-多糖共价复合物及其应用研究进展

蛋白质和多糖是食品中两类重要的生物大分子,是影响食品质构的主要因素,蛋白质具有乳化且稳定的能力,多糖主要是增稠和持水能力,但是做为添加剂使用时,在某些性能方面无法满足实际需要.蛋白质和多糖在控制条件下通过Maillard反应可发生一定程度的共价复合,而蛋白-多糖的共价复合物显示出比各自独立存在时更优越的性能.因此,蛋白质和多糖共价复合物成为近年来国内外食品科学界研究的一个焦点.本文综述了近年来国内外关于蛋白-多糖共价复合物的研究工作,简要介绍了蛋白-多糖共价复合物的制备方法、反应机理和组成结构,探讨了蛋白-多糖共价复合物的溶解性、乳化性、乳化稳定性、热稳定性、抗氧化性和抗菌性等功能性质,概括了蛋白-多糖共价复合物在众多领域的应用研究进展.     

蛋白质多酚多糖三元复合物的结构和功能特性研究进展

蛋白质-多酚-多糖三元复合物能够影响食品体系的感官、功能和营养等特性。本文主要关注在不同食品体系中,蛋白质、多酚和多糖三者之间通过非共价相互作用形成的三元复合物的结构和功能特性,总结蛋白质-多酚-多糖三元复合物对食品和饮料感官和功能等特性的影响,以及相关应用的科学问题,为更好理解蛋白质-多酚-多糖三元复合物在食品体系中的应用提供依据。     

多糖与蛋白质相互作用及其复合物的功能特性

多糖和蛋白质是食品中共存的生物大分子，营养丰富，两者相互作用可以改善食品的品质，因此成为研究的热点内容。该文对国内外有关多糖与蛋白质相互作用的研究进行综述，介绍多糖与蛋白质相互作用的类型、影响因素和复合物的制备方法、功能特性，并对其在食品中的应用进行展望，以期为多糖-蛋白质复合物的进一步研究与应用提供理论参考。     

魔芋葡甘聚糖/蛋白复合物的改性研究进展

由于食品组分中蛋白质、多糖之间的相互作用可以显示出比独立使用时更优越的性能,并影响食品体系的风味、营养、质构等品质,多糖/蛋白复合物研究正日益成为世界各国科技工作者研究的热点。文中以魔芋葡甘聚糖为代表多糖,探讨魔芋葡甘聚糖与相关蛋白复合物化学改性、物理改性和生物改性的研究进展,以及其改性后复合物体系功能变化,并对相关改性机制进行比较研究。     

蛋白质/多糖自组装及其应用

蛋白质和多糖,作为食品体系中最为重要的两种大分子,其自组装行为不仅影响食品品质,还在营养、药物递体系及软材料构建等方面有着广泛的应用。介绍蛋白质/多糖主要的自组装形式,包括复合物、纳米凝胶等,并简介蛋白质/多糖自组装在食品及其它领域的应用。     

多糖-蛋白复合作用研究进展

介绍了多糖对蛋白的稳定作用及相互作用对蛋白质功能性质的影响,并对近年来国外在该领域的研究动态进行了综述。     

蛋白质-多糖多尺度复合物结构的形成机制及其应用前景

蛋白质-多糖复合物结构的形成基础是分子间相互作用，包括共价和非共价相互作用。在特定加工条件下，由于分子间作用力的驱动，蛋白质和多糖可组装形成分子水平-微观水平-宏观水平上的多尺度复合物。而调控蛋白质-多糖复合物多尺度结构的形成，发挥不同组分的协同增效作用，对于设计具有特定或新功能的蛋白质-多糖复合物具有重要意义。本文以蛋白质与多糖分子间的相互作用为出发点，综述了蛋白质-多糖复合物多尺度结构的形成及其对功能特性的影响，同时介绍了蛋白质-多糖多尺度复合体系的应用前景，以期为设计和开发功能优异的蛋白质-多糖复合体系产品提供参考。     

大豆蛋白-瓜尔豆胶复合物乳化性能的研究

蛋白-多糖共价复合是一种有效改善蛋白质功能性质的方法,近十年来,研究人员对此进行了一系列研究。本文对大豆蛋白-瓜尔豆胶复合物的乳化性能进行了研究,发现复合物的乳化活性都比原大豆蛋白有所提高,在碱性、高温条件下乳化活性最好。     

Food‐Grade Covalent Complexes and Their Application as Nutraceutical Delivery Systems: A Review

Food proteins, polysaccharides, and polyphenols are 3 major food constituents with distinctly different functional attributes. Many proteins and polysaccharides are capable of stabilizing emulsions and foams, thickening solutions, and forming gels, although they differ considerably in their abilities to provide these functional attributes. Many plant polyphenols exhibit beneficial physiological functions, such as antitumor, antioxidant, antibacterial, and antiviral properties. Proteins, polysaccharides, and polyphenols can form complexes with each other, which leads to changes in the functional and nutritional properties of the combined systems. Recently, there has been considerable interest in understanding and utilizing covalent interactions between polyphenols and biopolymers (proteins and polysaccharides). The binary or tertiary conjugates formed may be designed to have physicochemical properties and functional attributes that cannot be achieved using the individual components. This article provides a review of the formation, characterization, and utilization of conjugates prepared using proteins, polysaccharides, and polyphenols. It also discusses the relationship between the structural properties and functionality of the conjugates, and it highlights the bioavailability of bioactive compounds loaded in conjugate‐based delivery systems. In addition, it highlights the main challenges to be considered when preparing and analyzing conjugates. This article provides an improved understanding of the chemical reactions that occur between major food ingredients and how they can be utilized to develop biopolymer‐based delivery systems with enhanced functional attributes.     

Formation of soy protein isolate–dextran conjugates by moderate Maillard reaction in macromolecular crowding conditions

BACKGROUND: Several methods have been reported for the conjugation of proteins with polysaccharides. Protein–polysaccharide conjugates can be formed by traditional dry heating, but this process is not attractive from an industrial viewpoint, and no commercial conjugates have been manufactured in this way. In the present study, in order to develop a more practical reaction method, macromolecular crowding was used to attach polysaccharides to proteins. RESULTS: Soy protein isolate–dextran conjugates (SDCs) were prepared via the initial stage of the Maillard reaction in macromolecular crowding conditions. The impact of various processing conditions on the formation of SDCs was investigated. The optimal conditions chosen from the experiments were a soy protein isolate/dextran ratio of 1:1 (w/w), a pH of 6.5, a reaction temperature of 60 °C and a reaction time of 30 h. Circular dichroism spectroscopy showed that the secondary and tertiary structures of the conjugates were changed significantly. Structural flexibility increased, allowing better display of their functional characteristics. The conjugates had a composition with various sizes, especially macromolecules, according to gel permeation chromatography. Thermal analysis showed that the thermal stability of the conjugates was improved. CONCLUSION: The production of SDCs under macromolecular crowding conditions appears to be an effective and promising technique, representing an advance over classic protein glycosylation methods. Copyright © 2012 Society of Chemical Industry     

Maillard反应合成蛋白质-多糖复合物及其应用

综述了利用美拉德反应制得的蛋白-多糖复合物的性能,这种复合物主要是在干燥状态下利用自发进行的美拉德反应制得的。同传统商业上使用的乳化剂相比,该复合物具有优良的乳化性能,热稳定性和抑菌性。因此,该复合物在工业上可以用作天然乳化剂,无毒抑菌剂。同时如果多糖与过敏原蛋白复合还具有减轻蛋白的致敏性的效果。     

Preparation and potential applications of casein–polysaccharide conjugates: a review

Glycation of casein and caseinates with polysaccharides via Maillard reaction is a simple and environmentally safe way to prepare new food ingredients of improved functional properties. Sodium caseinate has been used mainly to prepare conjugates with several polysaccharides particularly maltodextrins and dextrans. The functional properties of these conjugates are influenced by the used polysaccharides and heating conditions. Under optimal heating conditions substantial improvements have been evident in their emulsification and foam properties of these conjugates. Casein–polysaccharide conjugates have several potential applications in food processing and microencapsulation. This article gives an overview on their formation and potential uses. © 2019 Society of Chemical Industry     

美拉德反应合成蛋白质—多糖复合物及其应用

该文综述利用美拉德(Maillard)反应制得蛋白—多糖复合物性能,该复合物主要是在干燥状态下利用自发进行美拉德反应所制得,与传统商业使用乳化剂相比,该复合物具有优良乳化性、热稳定性和抑菌性。因此,该复合物在工业上可用作天然乳化剂、无毒抑菌剂;同时如为多糖与过敏原蛋白复合还具减轻蛋白致敏性效果。     

食品级共价复合物在递送生物活性物质方面的研究进展

生物活性物质由于具有抗肿瘤、抗炎、抗氧化和降血脂活性,是功能性食品开发的良好原料,但在生产加工和储存的过程中大多容易分解。为解决这一问题,围绕蛋白质、多糖和多酚设计了食品级的递送系统,形成的复合物改变了食品的功能和营养特性。本文综述了利用蛋白质、多糖、多酚为原料制备不同功能性质的二元或三元食品级复合物的共轭方法、表征和功能性质的研究进展,总结了复合物作为载体的主要类型,以及在生物活性物质传递系统中的应用,并总结了递送体系与人体胃肠道之间的相互作用,强调了在制备和分析复合物作为递送体系时要注意的主要问题并展望了其应用前景。     

Functional properties of isolated porcine blood proteins modified by Maillard’s reaction

Plasma proteins (albumin and immunoglobulins) and haemoglobin from porcine blood can be recovered from slaughterhouse waste. These proteins are employed as ingredients in food products on account of their functional properties. There are different methods to improve these properties, Maillard’s reaction probably being the most promising technique for food purposes. In the present study, 10 kDa dextran was employed to produce the conjugates. Three reaction temperatures were assayed, 80 °C for 60 min being found to be the most suitable to produce conjugates with enhanced functional properties. Both thermal stability and emulsification capacity were improved; gelling temperature was increased 15 °C; and gel strength was lowered 50% compared to native proteins. However, solubility decreased slightly. It has been demonstrated that the functional properties of blood proteins are enhanced through conjugation, showing a improvement in the application of the blood proteins in food products.     

Properties of acid gels made from sodium caseinate-maltodextrin conjugates prepared by a wet heating method

Covalent attachment of polysaccharides to proteins (conjugation) via the Maillard reaction has been extensively studied. Conjugation can lead to a significant improvement in protein functionality (e.g., solubility, emulsification, and heat stability). Caseins have previously been successfully conjugated with maltodextrin (Md), but the effect on the detailed acid gelation properties has not been examined. We studied the effect of conjugating sodium caseinate (NaCN) with 3 different sized Md samples via the Maillard reaction in aqueous solutions. The Md samples had dextrose equivalents of 4 to 7, 9 to 12, and 20 to 23 for Md40, Md100, and Md200, respectively. The conjugation reaction was performed in mixtures with 5% NaCN and 5% Md, which were heated at 90°C for 10 h. The degree of conjugation was estimated from the reduction in free amino groups as well as color changes. Sodium dodecyl sulfate-PAGE analysis was performed to confirm conjugation by employing staining of both protein and carbohydrate bands. The molar mass of samples was determined by size-exclusion chromatography coupled with multi-angle laser light scattering. After the conjugation reaction, samples were then gelled by the addition of 0.63% (wt/vol) glucono-δ-lactone at 30°C, such that samples reached pH 4.6 after about 13 h. The rheological properties of samples during acidification was monitored by small-strain dynamic oscillatory rheology. The microstructure of acid gels at pH 4.6 was examined by fluorescence microscopy. Conjugation resulted in a loss of 10.8, 8.8, and 11.9% of the available amino groups in the protein for the NaCN-Md40 conjugates (C40), NaCN-Md100 conjugates (C100), and NaCN-Md100 conjugates (C200), respectively. With a decrease in the size of the type of Md, an increase occurred in the molar mass of the resultant conjugate. The weight average molar masses of NaCN-Md samples were 340, 368, and 425 kDa for the conjugates C40, C100, and C200, respectively. Addition of Md to NaCN dispersion resulted in slightly shorter acid gelation times even without the conjugation reaction. The storage modulus (G′) of acid gels was significantly lower in conjugated samples compared with the corresponding (unreacted) mixtures of Md and NaCN. The sample with the lowest G′ value at pH 4.6 was the C40 conjugate. Fluorescence microscopy showed that gels made by conjugates had slightly larger pores. These results indicate that conjugation of casein modified its acid gelation properties, presumably by the Md polysaccharide moiety hindering aggregation and rearrangements of the casein network.     

Creating proteins with novel functionality via the Maillard reaction: a review

Proteins are widely utilized to add functional properties, such as gelling and emulsification to foods. These attributes depend on a number of factors such as molecular structure of the protein, the pH, and the composition of its chemical environment. There is substantial evidence to suggest that the functional properties of food proteins can be further improved by derivatization. Covalent bonding of proteins to polysaccharides and smaller reducing sugars via the Maillard reaction has been shown to alter the functionality of proteins without requiring the addition of chemical reagents. Establishment of a technologically feasible method for preparing the conjugates and optimization of the processing conditions, however, is needed to promote their development as functional food ingredients. This paper provides a state-of-the-art contribution to the impact of the Maillard reaction on protein functionality. It presents a deeper understanding of the influence of processing conditions and reactant formulation on improving desirable properties of proteins. In particular attention is given to how potential improvements could be achieved in the emulsifying, textural, and solubility properties of proteins to add value to commodity food ingredients. Elements that are considered to be critical to the design of functional Maillard conjugates are highlighted and suggestions proposed to facilitate progress in this area.     

Ultrasound assisted vis-à-vis classical heating for the conjugation of whey protein isolate-gellan gum: Process optimization,structural characterization and physico-functional evaluation

In the present work, ultrasonic assisted synthesis and characterization of Maillard conjugates of whey protein isolate (WPI) and gellan gum (GG) was carried out and compared with the classical heating method. Conjugation was confirmed by FTIR, secondary structure, intrinsic fluorescence analysis, and degree of glycation (DG). The structural analysis revealed high protein unfolding by sonication confirming loss of α-helix content and exposing more amino groups to the conjugation reaction. Color change analysis confirmed that ultrasonication accelerated the initial stage of Maillard reaction but did not form the advanced Maillard reaction products. Ultrasonication gave higher DG in lesser time (17.22% in 60 min) than classical heating method (8.41% in 4 h). Physico-functional properties such as pH and thermal stability, emulsifying activity index, emulsion stability index, foaming capability and antioxidant activity of WPI-GG conjugates prepared by ultrasonic treatment were superior to classical heating method suggesting ultrasonication as a potentially alternative method for Maillard conjugation.Industrial relevanceImprovising supplementary protein functionality by conjugation with food grade polysaccharides like gellan gum through ultrasonication could make the process more controllable and economical. The undesired browning can be inhibited in ultrasonic assisted conjugate synthesis and hence the overall acceptance of the final product can be increased.