Effect of beta-lactoglobulin A and B whey protein variants on the rennet-induced gelation of skim milk gels in a model reconstituted skim milk system

The effect of fortifying reconstituted skim milk with increasing levels of the β-lactoglobulin (β-LG) genetic variants A, B, and an A-B mixture on rennet-induced gelation was studied by small deformation-sensitive rheology. Free-zone capillary electrophoresis and high-sensitivity oscillatory rheology were used to elucidate the role of potential heterotypic associative interactions between whey proteins and casein in a mixed colloidal system, subjected to moderate heating (65°C for 30 min) prior to renneting, on the gelling properties of the system. Increasing levels of added whey protein, in the concentration range of 0.225 to 1.35% of added protein, led to a concomitant progressive increase in the equilibrium shear storage modulus, G′ (recorded after ∼10,800 s), in the order β-LG B > β-LG A and β-LG A-B, as the general expected consequence of the setup of denser casein gel networks. The preferential effect of β-LG B over β-LG A on the mechanical strength of the gels may be due to the formation of cross-links and aggregates involving whey proteins and rennet hydrolysis products or an increase in the size of the casein micelle caused by the grafting of β-LG B to its surface, or both. The results of free-zone capillary electrophoresis were consistent with the notion that β-LG B (and not β-LG A) binds to the casein micelle under an optimal stoichiometry of 1:0.045 (mg/mg), even in the absence of heat treatment. The liquid-like character of the gel networks formed, tan δ, was a parameter sensitive to the level of addition of β-LG A in particular. At low concentrations (up to 0.45%) of β-LG A, tan δ increased by almost twice as much, which was interpreted as a result of the increase in the loss modulus, G″, of the sol fraction because of the presence of unbound β-LG A. At greater incremental concentrations of β-LG (>0.45%), the formation of smaller whey protein aggregates confined to the sol fraction may have led to a progressive decrease in tan δ. The critical gel time, t_gel, was also affected by the concentration of added whey protein and described 3 zones of behavior, irrespective of the type of whey protein variant. The critical gel time was slightly shorter for β-LG B than for β-LG A at 0.45% of added whey protein, but this difference became larger at 0.67%. Even when only β-LG B was found to associate with casein prior to renneting, both β-LG A and β-LG B, either alone or mixed, had a profound influence on the mechanical strength and coagulation kinetics of the rennet-induced casein gels. This knowledge is expected to be useful to exert better control and optimize processing conditions during the manufacturing of cheese and cheese analogs.     

高压处理大豆分离蛋白水解物对羊肉糜凝胶特性及贮藏期氧化稳定性的影响

为研究添加不同高压处理(0.1、100、200、300 MPa)的大豆分离蛋白水解物(soy protein isolate hydrolysate, SPIH)对羊肉糜凝胶特性及贮藏期间氧化稳定性的影响,以未添加水解物的羊肉糜为对照组,测定了羊肉糜的质构、流变特性和微观结构,同时检测了在4℃贮藏8 d的过程中,羊肉糜的色差、酸价、硫代巴比妥酸值、羰基及总巯基含量。结果表明：与对照组相比,添加不同高压处理的SPIH的羊肉糜硬度、弹性及回复性显著提高(P<0.05);升温过程中,添加不同高压处理的SPIH的羊肉糜弹性模量G′均先下降后上升,且在整个升温过程中,SPIH处理压力为200 MPa时,羊肉糜的G′值始终最高;同一频率振荡下,添加200 MPa处理的SPIH的羊肉糜G′值也最高;扫描电镜结果显示,与对照组相比,添加水解物的羊肉糜结构更加致密均匀;随着贮藏时间的延长,添加不同压力下原料肉质量2.0%的SPIH能够抑制羊肉糜的b~*值(黄度)、酸价、硫代巴比妥酸值和羰基含量的上升以及L~*值(亮度)、a~*值(红度)和总巯基含量的下降,且200 MPa处理的SPIH抑制脂肪、蛋...     

黄油的研究进展

近年来国内黄油的贸易量、关注度和研究热度显著上升。黄油开发及创新面临着如何提升感官特性、健康品质和绿色发展水平等多重挑战。作者综述了黄油市场及国内外研究现状,分析了未来黄油研发的重点方向与解决方法,重点探讨了未来黄油的原料创新和技术创新方式,旨在为当前黄油生产和新型黄油开发提供参考。     

3种淀粉对鸡肉糜盐溶蛋白特性影响及其配方研究

为获得鸡肉蛋白较好的凝胶特性,从而改善其肉糜的加工品质,探讨玉米淀粉、马铃薯淀粉和磷酸酯淀粉3种常用淀粉与鸡肉盐溶蛋白相互作用对鸡肉糜加工基本特性的影响。以盐溶蛋白析出质量浓度、活性自由巯基含量和相对疏水性为指标,分别研究单因素条件下3种淀粉对鸡肉盐溶蛋白特性的影响,并通过二次通用旋转试验筛选出在5%淀粉添加总量条件下3种淀粉在鸡肉糜中的最佳组合配方。单因素试验表明:所选3种淀粉均对鸡肉盐溶蛋白特性有着复杂影响。3种淀粉最佳配方为:玉米淀粉1.6%、马铃薯1.6%、磷酸酯淀粉1.8%,此时鸡肉糜中盐溶蛋白基本特性参量指标预计为:盐溶蛋白质量浓度24.3mg/mL,活性自由巯基含量0.004μmol/mg,相对疏水性值22.86。     

大豆分离蛋白凝胶制备和凝胶质构特性研究

本研究以大豆分离蛋白为原料，考察蛋白质浓度、pH值、加热温度、加热时间对凝胶形成的影响，采用物性仪对不同务件下制备的凝胶的质构特性进行研究，不同评价指标得出的结论不尽相同。通过正交实验得出形成凝胶硬度最大的制备条件为：蛋白浓度12％，pH值6．5，加热温度95℃，加热时间35min；形成凝胶脆性最大的制备凝胶争件为：蛋白浓度12％，pH值7．0，加热温度95℃，加热时间25min；形成凝胶弹性最好的制备凝胶务件为：蛋白浓度12％，pH值7．0，加热温度85℃，加热时间35min；形成凝胶粘附性最大的制备凝胶条件为：蛋白浓度12％，pH值7．0，加热温度95℃，加热时间35min。     

Protective Effect of Microencapsulation Consisting of Multiple Emulsification and Heat Gelation Processes on Immunoglobulin in Yolk

ABSTRACT: Two different emulsification methods involving multiple emulsification and heat gelation were used for preparation of whey protein-based microcapsules containing immunoglobulin in yolk (IgY). The residual activity of IgY during the emulsion preparation and the effects of microencapsulation on IgY stability under harsh conditions were investigated. The residual activity of IgY in an emulsion prepared with a membrane emulsifier was higher than for an emulsion using a homogenizer. Microencapsulated IgY showed remarkable stability against both pepsin and acid. Both microencapsulated IgY and nonencapsulated IgY were relatively stable in bile and artificial intestinal juice. Microencapsulated IgY retained 74% of initial activity during heat treatment. There were no significant differences in the residual activities of microencapsulated IgY under storage temperatures of 4, 25, and 37°C.     

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。     

加热模式对添加葡萄糖氧化酶鲢鱼糜凝胶特性的影响

研究两段法加热模式对添加葡萄糖氧化酶鲢鱼糜凝胶特性的影响。结果表明,在凝胶化阶段,高温短时（40 ℃、1 h）模式下,鱼糜凝胶强度、持水性、白度和不易流动水含量最高,且自由水含量最低,凝胶网络结构最致密;十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE）图谱显示,在高温短时（40 ℃、1 h）模式下,肌球蛋白重链（myosin heavy china,MHC）条带强度降低,说明此时蛋白降解较多。在熟化阶段时,微波加热鱼糜凝胶的凝胶强度、持水性和白度最高,三氯乙酸-溶解肽含量、自由水含量和孔隙当量直径最小,形成了有序致密的三维网络结构;SDS-PAGE图谱显示,相比水浴加热,微波加热下MHC条带强度更高,说明微波加热促进了二硫键的形成。因此,适宜的加热模式能改善鱼糜凝胶的品质。     

Improving gelling properties of myofibrillar proteins incorporating with cellulose micro/nanofibres

The effects of cellulose microfibres (CMFs, Average size: 100 ± 5 μm) and cellulose nanofibres (CNFs, Average size: 60 ± 3 nm) on the properties of myofibrillar protein (MP) gels from duck breast meat were studied. The results demonstrated that CMFs and CNFs were mostly connected to MP by non-covalent bonds, the diffusion and cross-linking of MP molecules was promoted, and a denser and more complete gel network was formed. With the increases of CMFs and CNFs concentration (0–10%), the hardness was increased by 13.15% and 19.78% for CMFs10% and CNFs10% gels, respectively, and the elasticity was increased by 40% and 80%, respectively. At the same concentration (0–10%), the increase in gel hardness, viscoelasticity and immobilised water content was greater in the CNFs-MP group than in the CMFs-MP group. The CNFs-MP group had a tighter gel network, and CNFs had a better potential to improve the gelation performance of MP.     

Effect of microwave heating time on the gel properties of chicken myofibrillar proteins and their formation mechanism

The present work was conducted to illustrate the mechanism of gel formation of myofibrillar proteins (MPs) under different microwave heating times. The results showed that the denaturation enthalpy (ΔH) of the MPs significantly decreased when the heating time increased from 3 to 9 s and then completely disappeared as the heating time progressed, indicating that the MPs gradually denatured and subsequently aggregated with increasing heating time, which was further verified by the changes in the secondary structure, electrophoretic bands, and gel properties (e.g., water holding capacity and textural profiles) of the MPs. Microstructural images indicated that the MP gel formed under 12 s had the most compact network, indicating that extended microwave heating time could induce quality deterioration of MP gels. Moreover, the hydrophobic forces, electrostatic forces, and disulphide bonds of the MPs gradually intensified with increasing microwave heating time, suggesting that both non-covalent and covalent bonds could promote molecular denaturation and subsequent aggregation of MPs. In addition, correlation analysis revealed that the changes in the molecular conformation of MPs induced by different microwave heating times could effectively regulate the formation of MP gels and their related properties.