Physicochemical and antioxidant properties of Maillard reaction products formed by heating whey protein isolate and reducing sugars

This study was conducted to investigate the physicochemical and antioxidant properties of Maillard reaction products (MRP) prepared by heating whey protein isolate (WPI) and reducing sugars (glucose and galactose) to 95 °C for different lengths of time (0–6 h). The results revealed that the colour, intermediate products, browning intensity and the antioxidant activities of the MRP increased as the reaction time increased (P < 0.05), whereas the pH value and free amino group content decreased (P < 0.05). Sodium dodecyl sulphate–polyacrylamide gel electrophoresis indicated that the covalently linked conjugates of WPI and sugars were formed. The results indicate that the Maillard reaction could improve the antioxidant capacity of WPI.     

Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction

Reaction mixtures containing peanut protein isolate (PPI) and dextran (1:1 weight ratio) were dry-heated at 60 °C and 79% relative humidity for 7 days. SDS-PAGE analysis indicated that PPI had become complexed with dextran to form conjugates of higher molecular weight. Arachin, accounting for 50% of peanut proteins, was hard to glycosylate with dextran, which might limit the extent of glycosylation of PPI. The thermal stability of PPI was remarkably improved by mixture/conjugation with dextran. Proteins in mixtures/conjugates might have a more compacted tertiary conformation than PPI. The protein solubility of conjugates at pH 4.5-6.0 was remarkably increased compared with the PPI/mixture. Mixture with dextran could significantly improve the emulsifying and foaming properties of PPI (p < 0.05). Conjugation with dextran could further enhance emulsifying and foaming properties of PPI.     

Improvement in emulsifying properties of soy protein isolate by conjugation with maltodextrin using high‐temperature,short‐time dry‐heating Maillard reaction

Soy protein isolate (SPI)–maltodextrin (MD) conjugates were synthesised using Maillard reaction under high‐temperature (90, 115 and 140 °C), short‐time (2 h) dry‐heating conditions. The loss of free amino groups in proteins and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) profile confirmed that SPI‐MD conjugates were formed and higher dry‐heated temperatures could increase the glycosylation degree. The emulsifying properties of SPI and SPI‐MD conjugates were evaluated in oil‐in‐water emulsions. The emulsions stabilised with SPI‐MD conjugates synthesised at 140 °C exhibited higher emulsifying stability and excellent storage stability against pH, ionic strength and thermal treatment compared with those synthesised at 90 °C, 115 °C and SPI stabilised emulsions. This might be due to a greater proportion of conjugated MD in SPI‐MD conjugates synthesised at 140 °C because of the higher glycosylation degree, and more conjugated MD on the droplet surface could provide steric effect and enhance the stability of the droplets in the emulsions.     

湿热条件下低聚木糖-乳清分离蛋白的美拉德反应及产物乳化性与流变性研究

本文研究了湿热条件下不同混合质量比(1:1、1:2、1:3、1:4,W/W)对低聚木糖与乳清分离蛋白(WPI)美拉德反应及其产物的乳化性与流变性的影响。UV-Vis吸光度值,pH和粒径大小显著变化表明,该条件下成功制备了WPI和低聚木糖的美拉德反应产物 (MRPs)。数据显示,质量比为1:2的溶液体系美拉德反应程度最高;与未经过美拉德反应的体系相比,MRPs的平均粒径均减小而质量比为1:2的体系平均粒径最大;同时,美拉德反应提高了WPI的乳化活性和乳化稳定性,比例为1:2时MRPs具有最佳的乳化活性(38.63 m2/g)和乳化稳定性(65.23%);流变学测试表明糖基化修饰增强了WPI的凝胶性,比例为1:3时MRPs的储存模量提高最大,G''值高达约97,000 Pa (约WPI的7倍);在相同剪切速率下,MRPs溶液的表观粘度增加,而WPI的添加比例对体系粘度的影响占主导作用。上述研究表明,美拉德反应可改善WPI的乳化特性和凝胶特性。     

不同酶切方式对乳清蛋白疏水性和乳化性的影响

采用不同的蛋白酶对乳清蛋白进行水解,考察了肽键断裂方式对乳清蛋白肽疏水性和乳化性的影响,以及乳清蛋白不同酶解产物的疏水性和乳化性的关系。结果表明:不同蛋白酶作用于乳清蛋白得到的水解产物疏水性不同,6种蛋白酶解液的疏水性均随水解度的增大而降低,其中以胰凝乳蛋白酶酶解液的疏水性下降的最慢。研究还发现,乳化性随着水解度增加而先升高后下降,以双酶复合酶解液最差。不同蛋白酶水解液的乳化性指数随疏水性指数的降低而升高,乳化性指数与疏水性氨基酸质量分数成正相关。     

Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation

The application of mung bean protein in foods is limited due to its poor functionality. Acylation with succinic anhydride could be used to improve the functionalities of protein. In this study, the influence of the weight ratio of succinic anhydride to protein (0–0.10) on the degree of N-acylation, physicochemical properties and protein functionalities including emulsifying properties of mung bean protein isolates (MPI) were investigated. The extent of N-acylation of MPI increased as the succinic anhydride:protein ratio increased, while the ζ-potential at neutral pH decreased. In addition, succinylation had an impact on the average particle size of MPI depending on the succinic anhydride:protein ratio. Succinylation had no impact on the total and exposed free sulfhydryl groups. Moreover, the isoelectric point (pI) of the succinylated proteins shifted from pH 5 to lower pH. Succinylation increased the emulsifying activity index (EAI), while the impact on the emulsion stability index depended on the succinic anhydride:protein ratio. Thus, succinylation at low succinic anhydride:protein ratio can alter mung bean protein charge and affect physicochemical and functional properties especially emulsifying properties that could be used to increase its utilization.     

大豆分离蛋白美拉德反应研究进展

本文首先综述了美拉德反应对大豆分离蛋白的溶解性、乳化性以及凝胶性等一系列功能特性的影响,进而阐述了美拉德反应对大豆分离蛋白生物活性的影响,如抗氧化性和抗菌性。最后对大豆分离蛋白的美拉德反应在食品领域的研究进行了展望,以期对大豆分离蛋白的美拉德反应在食品领域的研究提供参考。     

Anti-inflammatory activities of Maillard reaction products from whey protein isolate fermented by Lactobacillus gasseri 4M13 in lipopolysaccharide-stimulated RAW264.7 cells

Maillard reaction products formed from whey protein isolate (WPI) and sugar have been shown to have an anti-inflammatory effect in vitro. Here, we incubated WPI and galactose (GWA) in an aqueous solution at 65°C for 24 h to produce a glycated conjugate, which was then fermented using Lactobacillus gasseri 4M13 to obtain the fermented product (F-GWA). We demonstrated that F-GWA had an anti-inflammatory effect on lipopolysaccharide (LPS)-stimulated RAW264.7 cells. It reduced both LPS-stimulated nitric oxide production and LPS-stimulated increases in the gene expression levels of tumor necrosis factor-α and cyclooxygenase-2 in a dose-dependent manner. Furthermore, F-GWA inhibited the LPS-induced phosphorylation of extracellular signal-regulated kinase and c-Jun N-terminal kinase, members of the mitogen-activated protein kinase family. The glycation process was evaluated by measuring fluorescence intensity and the furosine concentration during the Maillard reaction to form GWA. The protein modifications of WPI were analyzed using MALDI-TOF tandem mass spectrometry. We found that the combination of the Maillard reaction and L. gasseri 4M13 fermentation increased the prebiotic properties of GWA as well as organic acid production, compared with the nonreacted WPI and galactose.     

玉米胚芽分离蛋白溶解性和乳化性质的研究

以湿法脱胚的玉米胚芽为原料,采用碱溶酸沉法制备了玉米胚芽分离蛋白。探讨了不同实验条件如温度、pH、盐浓度等对玉米胚芽分离蛋白的溶解性和乳化性的影响,并解释了乳化性和溶解性在实验条件下的变化规律。研究结果表明,玉米胚芽分离蛋白在碱性条件下溶解度较好,55℃时溶解度最大;在pH 7.0~8.5范围内乳化活性明显增加,提高温度可以增加蛋白质的乳化活性。     

Incorporated glucosamine adversely affects the emulsifying properties of whey protein isolate polymerized by transglutaminase

Glucosamine (GlcN) and microbial transglutaminase (Tgase) are used separately or together to improve the emulsifying properties of whey protein isolate (WPI). However, little is known about how the emulsifying properties change when GlcN residues are incorporated into WPI cross-linked by Tgase. We used Tgase as a biocatalyst to cross-link WPI in the presence of GlcN in a liquid system for 12 h at a moderate temperature (25°C). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analyses indicated that protein polymerization and GlcN conjugation occurred simultaneously, phenomena also supported by the loss of free amines (9.4–20.5%). Addition of 5 U Tgase/g protein improved the emulsifying properties of moderately cross-linked WPI polymers. The Tgase-treated WPI polymers had a larger particle size (～2.6-fold) than native WPI, which may have reduced coalescence and flocculation in an oil-in-water emulsion system. However, the incorporation of GlcN residues into WPI, predominantly via enzymatic glycation, partly inhibited the cross-links between the WPI molecules catalyzed by Tgase, reducing the size of the WPI polymers 0.81- to 0.86-fold). Consequently, WPI+GlcN conjugates provided less stability to the emulsion. Moreover, high NaCl concentration (0.2 M) decreased the emulsifying properties of the WPI+GlcN conjugates by neutralizing negative electric charges in the glycoconjugates. However, the improved emulsifying properties of WPI cross-linked by Tgase may be useful in food processing at higher NaCl concentrations due to the formation of the thicker steric barrier at the oil-water interface.     

Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating

Whey protein isolate (WPI) was glycated with maltopentaose (MP) through the Maillard reaction, and the MP-conjugated WPI (MP-WPI) was then phosphorylated by dry heating in the presence of pyrophosphate. Glycation occurred efficiently, and the sugar content of WPI increased approximately 19.9% through the Maillard reaction. The phosphorylation of MP-WPI was enhanced with an increase in the dry-heating time from 1 to 5 d, and the phosphorus content of WPI increased approximately 1.05% by dry heating at pH 4.0 and 85°C for 5 d in the presence of pyrophosphate. The electrophoretic mobility of WPI increased with an increase in the phosphorylation level. The stability of WPI against heat-induced insolubility at pH 7.0 was improved by conjugation with MP alone, and further improved by phosphorylation. Although the emulsifying activity of WPI was barely affected by glycation and phosphorylation, the emulsifying stability of phosphorylated MP-WPI (5 d), was 2.2 times higher than that of MP-WPI. Gelling properties such as hardness, resiliency, and water-holding capacity of heat-induced WPI gel were markedly improved, and the gel was rendered transparent by phosphorylation. The calcium phosphate-solubilizing ability of WPI was enhanced by phosphorylation. These results suggested that phosphorylation by dry heating in the presence of pyrophosphate after conjugation with MP is a useful method for improving the functional properties of WPI.     

糖基化反应对乳清蛋白-乳糖复合物乳化性的影响

糖基化反应是改善蛋白质功能特性的一种有效方法.研究了糖基化反应对乳清蛋白-乳糖复合物乳化性的影响.结果表明,糖基化反应能够改善乳清蛋白-乳糖复合物的乳化性和乳化稳定性.     

大豆分离蛋白起泡性和乳化性影响因素的研究

大豆分离蛋白的乳化性和起泡性与蛋白质、NaCl、卡拉胶、蔗糖和山梨酸钾含量、pH值、加热温度等密切相关。蛋白质质量浓度分别为2.0g/100mL和2.5g/100mL时,大豆分离蛋白乳化性和起泡性分别达到最大值;远离pH4.5,大豆分离蛋白起泡性和乳化性增加;加热温度45℃时起泡性最好,而乳化性最差;氯化钠、卡拉胶、山梨酸钾添加量分别为1.00g/100mL、0.20g/100mL、0.08g/100mL时,起泡性和乳化性好;添加蔗糖会使蛋白质的起泡性下降,而蔗糖添加量6.0g/100mL时乳化性好。     

Effects of process variables and addition of polydextrose and whey protein isolate on the properties of barley extrudates

Extrusion cooking is commonly used in the production of snacks. In the present study, extrudates were prepared using barley flour alone and with the addition of either polydextrose (PD) or whey protein isolate (WPI) and both PD and WPI. Independent process variables were water content of the mass (17%, 20% and 23%), screw speed (200, 350 and 500 rpm) and temperature of section 6 and die (110, 130 and 150 °C). Expansion, hardness, water content, porosity and chemical composition of the extrudates were analysed. Highly porous and expanded snack products with high dietary fibre and protein contents were obtained from barley flour and WPI when water content of mass was 17%, screw speed 500 rpm and temperature of section 6 and die 130 °C. Barley flour alone or with PD resulted in hard and non‐expanded extrudates. Expansion of extrudates was statistically significantly increased with decreasing water content of the mass and increasing screw speed in all trials.     

美拉德反应对豌豆蛋白水解物乳化性和抗氧化性的影响

本文考察了美拉德反应对不同商业蛋白酶（碱性蛋白酶、风味蛋白酶和复合蛋白酶）制备的豌豆蛋白水解物的理化性质、乳化性和抗氧化性的影响。豌豆蛋白水解物分别与葡萄糖、麦芽糊精和葡聚糖在pH7.0,60℃保温48h。结果:体系反应48h后游离氨基含量下降;希夫碱含量增加;反应物荧光强度下降。表明,豌豆蛋白水解物与糖发生了共价结合。SDS-PAGE进一步证实了高分子共聚物的生成。美拉德反应显著提高了风味蛋白酶和复合蛋白酶水解物的乳化能力,尤其是复合蛋白酶水解物与葡聚糖的反应产物表现出了极好的乳化活性和乳化稳定性。各美拉德反应产物均具有显著抑制脂质体氧化的能力（p<0.05）。所有糖中,葡聚糖制备的反应物具有最高的乳化活性和抗氧化活性。因此,葡聚糖参与的美拉德反应可作为提高豌豆蛋白水解物乳化性的一种有效方法,并完好保留水解物的抗氧化活性。      

Reducing the stiffness of concentrated whey protein isolate (WPI) gels by using WPI microparticles

Concentrated protein gels were prepared using native whey protein isolate (WPI) and WPI based microparticles. WPI microparticles were produced by making gel pieces from a concentrated WPI suspension (40% w/w), which were dried and milled. The protein within the microparticles was denatured and the protein concentration after drying was similar to the native WPI powder. WPI microparticles had irregular shape with an average size of about 70 μm. They absorbed water when dispersed in water, but the dispersion did not gel upon heating. Replacing part of the native WPI powder with WPI microparticles in the protein gel resulted in lower gel stiffness compared with a gel with the same overall protein concentration but without microparticles. However, microparticles also strengthened the continuous phase because they take up water from this phase. This might increase gel stiffness more than would be expected from an inert particle/filler. There was also good bonding between the microparticles and the WPI continuous phase in the gel, which contributed to gel stiffness.     

大豆分离蛋白及其美拉德反应产物成膜条件探究

本论文研究不同p H（10、11、12）、不同加热温度（70、80、90℃）和不同甘油浓度（0³.0 m L/100 m L）对浓度为6 g/100 m L大豆分离蛋白溶液及大豆分离蛋白-葡萄糖（w/w=1）美拉德反应溶液、大豆分离蛋白-木糖（w/w=1）美拉德反应溶液成膜条件的影响。通过测定大豆分离蛋白-葡萄糖/木糖溶液的色差值及吸光值来判断美拉德反应程度,通过肉眼和手感观察和评价膜的可揭性、颜色和表观特征。实验结果表明:当大豆分离蛋白和糖浓度均为6 g/100 m L的条件下,大豆分离蛋白的成膜条件为甘油浓度:2.5 m L/100 m L、溶液p H11、80℃加热60 min;大豆分离蛋白与木糖美拉德反应产物成膜条件为甘油浓度:0.125 m L/100 m L、溶液p H11、80℃加热60 min;而大豆分离蛋白与葡萄糖在此条件下美拉德反应程度不明显,因此未对其进行膜的制备。      

乳清分离蛋白与壳聚糖美拉德反应初级阶段产物乳化性研究

采用干热美拉德反应制备乳清分离蛋白(WPI)-壳聚糖复合物,通过对复合物的乳液粒径及稳定性分析,研究反应温度、WPI与壳聚糖质量比及反应时间对复合物乳化性的影响。荧光光谱分析表明：WPI和壳聚糖在干热反应后发生共价交联并且结构发生了变化。WPI与壳聚糖在50℃、相对湿度79%干热条件下,反应1～4d的产物为Maillard反应初级阶段产物,该产物的乳化性质得到改善。其中,WPI与壳聚糖以质量比1:4混合,50℃反应1d的产物乳化稳定性是反应前的10倍。