Preparation of Transparent Egg White Gel with Salt by Two-step Heating Method

A heat-induced transparent gel from egg white was prepared at low pH and low ionic strength by a one-step heating method. The addition of NaCl to the egg white formed a turbid gel on heating. Egg white, first diluted with water, gave a transparent solution upon heating of this mixture. The solution formed a transparent gel when heated with NaCl up to a concentration of 0.3M for a second time. The transparent gel obtained at 150 mM NaCl was more firm and less adhesive than the turbid gel prepared by the one-step heating method at the same pH, protein concentration, and NaCl concentration.     

Preparation of Heat-induced Transparent Gels from Egg White by the Control of pH and Ionic Strength of the Medium

Egg white was dialyzed against distilled water or diluted with water, and the precipitates formed were removed by centrifugation. The supernatant gave a transparent gel after being heated at an acidic pH (2–4). At other regions of pH, except for the highly alkaline region, the gel or suspension was turbid upon heating. Insufficient centrifugation of the dialyzed egg white or the addition of NaCl to the supernatant after centrifugation resulted in a turbid gel on heating at even acidic pH. The removal of the slight precipitate formed at low ionic strength and the maintenance of low ionic strength during heating were both necessary for production of a transparent gel.     

Formation of two types of gels from bovine myosin

Myosin was isolated from bovine m. semimembranosus and gels were formed by heat treatment at different pH values and ionic strengths. The gels were subjected to rigidity measurements and their microstructure was studied by scanning electron microscopy. This article provides evidence that myosin can form two completely different gel structures in the pH range 5.5–6.0, depending on ionic strength. Fine stranded gel structures were formed at low ionic strength (0.25M KCl), whereas coarsely aggregated gel structures were formed at high ionic strength (0.6M KCl). The fine stranded structure had a higher rigidity than the coarsely aggregated structure. It was found that all fine strand myosin gels were formed from turbid solutions and the aggregate gels from clear solutions. When the pH was lowered to 4 in 0.6M KCl a strand-type gel structure formed spontaneously on dialysis, even without heat treatment. This structure did not change in character on heating. It was concluded that the conditions required for the formation of strand-type myosin gels were already present before the heat treatment and that the strands were made up of myosin filaments at certain pH and ionic strength combinations, which produced a turbid solution. The strand-type structures were considered specific with regard to myosin interactions which was not the case for the aggregated structures. Variation of the heating temperature in the range 55 to 65°C had no major effect on the type of structure formed.     

Comparison of Transparent Gels with Turbid Gels Prepared from Egg White: Creep Analysis of Gels

Egg white from which the precipitate occurring during dialysis against water had been removed gave a transparent gel on heating at lower salt concentrations and pH 3.54. The addition of NaCl or a shift of pH from 3.54 to 4.50 brought about the turbid gels. Creep analyses of these transparent and turbid gels were done using a four-element mechanical model. The instantaneous elastic modulus, E₀, Newtonian modulus, ηn and retarded viscoelastic moduli, E₁ and η₁ increased with NaCl up to 125 mM and then decreased with increase in NaCl concentration at pH 3.54. At 125 mM NaCl and pH 3.54, a translucent gel was obtained. E₀ and η₁ decreased with the temperature of the gel, while E₁ and η₁did not change depending of temperature.     

Role of Reduced Ionic Strength and Low pH in Gelation of Chicken Breast Muscle Protein

ABSTRACT: Elastic gels with a high moisture content of 88% were prepared at an acidic pH and low ionic strength. The relationship among pH, ionic strength, water-holding capacity, and fold score of gels was investigated. A decrease of pH from 4.1 to 3.7 or below increased gel elasticity and significantly decreased water loss under pressure ( P < 0.05). In the presence of sodium chloride, gels made at pH 3.5 to 3.7 had decreased elasticity and increased water loss under pressure. Prior freezing increased the water loss of gels under pressure. Gels made with phosphoric acid and hydrochloric acid lost less water under pressure than those made with citric acid. The percentage loss of water from cylindrical gels was inversely related to the height of the cylinders, suggesting that surface effects were involved. These results suggest that net positive charges on the protein molecules at low pH produced electrostatic repulsion, which was a major driving force for water uptake in the low-salt gels.     

Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine

Binding properties are important for meat products and are substantially derived from the heat-induced gelation of myosin. We have shown that myosin is solubilized in a low ionic strength solution containing l-histidine. To clarify its processing characteristics, we investigated properties and structures of heat-induced gels of myosin solubilized in a low ionic strength solution containing l-histidine. Myosin in a low ionic strength solution formed transparent gels at 40-50 °C, while myosin in a high ionic strength solution formed opaque gels at 60-70 °C. The gel of myosin in a low ionic strength solution with l-histidine showed a fine network consisting of thin strands and its viscosity was lower than that of myosin in a high ionic strength solution at 40-50 °C. The rheological properties of heat-induced gels of myosin at low ionic strength are different from those at high ionic strength. This difference might be caused by structural changes in the rod region of myosin in a low ionic strength solution containing l-histidine.     

Role of Heavy Meromyosin in Heat‐Induced Gelation in Low Ionic Strength Solution Containing l‐Histidine

The gelation of myosin has a very important role in meat products. We have already shown that myosin in low ionic strength solution containing l ‐histidine forms a transparent gel after heating. To clarify the mechanism of this unique gelation, we investigated the changes in the nature of myosin subfragments during heating in solutions with low and high ionic strengths with and without l ‐histidine. The hydrophobicity of myosin and heavy meromyosin (HMM) in low ionic strength solution containing l ‐histidine was lower than in high ionic strength solution. The SH contents of myosin and HMM in low ionic strength solution containing l ‐histidine did not change during the heating process, whereas in high ionic strength solution they decreased slightly. The heat‐induced globular masses of HMM in low ionic strength solution containing l ‐histidine were smaller than those in high ionic strength solution. These findings suggested that the polymerization of HMM molecules by heating was suppressed in low ionic strength solution containing l ‐histidine, resulting in formation of the unique gel.     

Enzymatic modification of selected functional properties of myofibril preparation obtained from mechanically recovered poultry meat

The effect of addition of 3 g/L of commercially available transglutaminase preparation to protein extracts obtained from mechanically recovered poultry meat was studied. The content of free thiol groups (–SH), thermal drip and gel texture were determined. After pre-incubation at 7–8 °C for 1, 3, 5 and 24 h, the samples were subjected to one-step heating at 50, 60, 70 and 80 °C and two-step heating at 50/80, 55/80 and 60/80 °C. The addition of preparation and the extension of pre-incubation time led to decrease of free -SH groups content. After heating, the number of thiol groups decreased, the texture was improved, but thermal drip from gels increased. The amount of –SH groups in gel extracts subjected to one-step heating decreased with simultaneous increase of mechanical strength of gels. Protein gels subjected to two-step heating exhibited higher firmness than gels subjected to one-step heating. Thus, the 3 g/L addition of transglutaminase preparation in combination with one-step thermal processing at 70 °C and pre-incubation for 3 h contributed to improvement of texture properties of model gels and low thermal drip.     

影响猪血浆蛋白热诱导凝胶质构特性及持水性因素的研究

本实验研究在一定的加热条件下猪血浆蛋白质量浓度、加热温度、加热时间、离子种类、离子强度和pH 值对猪血浆蛋白热诱导凝胶的质构、持水性等性质的影响。利用质构仪测定猪血浆蛋白热诱导凝胶的硬度和黏附性,利用离心的方法测定凝胶的持水性。结果表明,在80℃下加热45min,猪血浆蛋白质量浓度超过6g/100mL可以形成凝胶,并且随蛋白质量浓度的增大,凝胶强度和持水性也增大;凝胶强度随pH 值(3～9)增加而增大,pH5 时凝胶的持水性最小,pH3 时最大;NaCl 浓度0.2mol/L,CaCl2 浓度0.6mol/L 时,凝胶硬度最大。实验得出,猪血浆蛋白热诱导凝胶的质构特性及持水性受许多因素影响,在实际生产中应该控制加热条件,以获得高质量的凝胶。     

Protein Components Precipitated from Egg White by Removal of Salt

A precipitate that formed in egg white at low ionic strength affected the transparency of heat-induced gels prepared at pH 2-4 and low ionic strength. The precipitate solubilized with SDS solution containing 2-mercaptoethanol and urea included major proteins of the egg white, as shown by SDS-polyacrylamide gel electrophoresis. The bands of ovalbumin, conalbumin and other protein were smaller when the precipitate was washed with water, but lysozyme and ovomacroglobulin probably remained in the precipitate fraction. It seemed that ovalbumin, conalbumin, and other proteins co-precipitated with these two kinds of proteins. Lysozyme added to the supernatant of egg white after dialysis, did not appear to produce turbidity upon heating at pH 2.5, but whole egg white was converted to a turbid gel upon being heated at this pH.     

咸味肽（鸟胺牛磺酸）添加量对低钠肉糜热凝胶特性的影响

研究咸味肽（鸟胺牛磺酸）添加量对低钠肉糜热凝胶特性的影响。采用单因素试验研究pH值（6.0～7.2）对50%咸味肽替代后的肉糜热凝胶质构特性和保水性能的影响。在单因素试验的基础上,利用完全随机排列试验,研究咸味肽替代比例（30%、40%、50%）和pH值（6.0、6.5、7.0）对肉糜热凝胶质构特性和保水性能的影响。结果表明：在2.5%的离子强度和50%咸味肽替代比例下,pH值的变化（6.0～7.2）对肉糜热凝胶的质构有显著影响,对保水性影响不显著。咸味肽使用会对肉糜的质构及保水性质产生不利的影响,但调节pH值至偏中性条件在一定程度上可降低咸味肽的不利作用。     

Role of pH and Ionic Strength on Water Relationships in Washed Minced Chicken-breast Muscle Gels

ABSTRACT The relationship between pH, ionic strength, and water balance of chicken-breast muscle gels was investigated. An increase in gel pH (pH 6.4 to 7.4) without added NaCl led to dramatic increases in water-holding capacity and water uptake (P < 0.05). Gels at 150 mM NaCl exhibited less ability to adsorb water than salt-free gels (P < 0.05 at pH 6.8 to 7.4) and had lower water-holding capacities (P < 0.05) and fold scores at and below pH 7. Varying salt concentration of the gel-bathing solutions had dramatic effect on the water uptake of the gels. The results show that strong water-absorbing gels can be produced at low ionic strengths and suggest that the negative charge of the muscle proteins is the driving force for water uptake and retention.     

原子力显微镜研究L-半胱氨酸对鲢肌球蛋白溶液热聚集行为的影响

利用原子力显微镜技术分析L-半胱氨酸（L-cysteine,L-Cys）对鲢肌球蛋白热聚集行为的影响。在肌球蛋白溶液中添加5?mmol/L（pH?7.0）的L-Cys溶液,分别进行未加热（25?℃、30?min）、一段式加热（90?℃、30?min）、二段式加热（40?℃、60?min＋90?℃、30?min）处理,分别测定溶解度、表面疏水性、聚集行为表面形貌的变化。结果表明：3?种加热方式低盐条件下L-Cys均显著提高肌球蛋白的溶解度（P＜0.05）;一段式加热时L-Cys显著提高高/低盐条件下肌球蛋白的表面疏水性（P＜0.05）,二段式加热时高盐条件下表面疏水性显著提高（P＜0.05）,其他条件下表面疏水性无明显变化。高/低盐条件下添加L-Cys均能显著改变肌球蛋白聚集行为的表面形貌,使聚集体更加分散,抑制了肌球蛋白的聚集。L-Cys对肌球蛋白溶解度、表面疏水性的影响进一步影响了其聚集行为,改变其聚集形貌。     

Heat-induced gelation of whey protein at high pH studied by combined UV spectroscopy and refractive index measurement after size exclusion chromatography and by in-situ dynamic light scattering

Summary The interactions between β-lactoglobulin and α-lactalbumin involved in gelation at 67.5 °C at high pH and low salt concentration were studied by size exclusion chromatography, followed by UV and refractive index measurements, and by in-situ dynamic light scattering. This was achieved by choosing whey protein samples with different proportions of the two proteins. The ratio of absorbance at 280 nm to the refractive index was used to demonstrate that α-lactalbumin was incorporated in aggregates and gels and drastically changed the properties of the gel, making them much more turbid than the transparent gels formed by β-lactoglobulin alone at the same pH and ionic strength. At a ratio of 1:2 for α-lactalbumin relative to β-lactoglobulin in the samples, the gel consisted of a 1:1 mixture of the two proteins. The aggregates present after 10 min of heating at 67.5 °C had molar mass of about 6.10⁶ g/mol and a radius of gyration of about 40 nm. After gel formation the field autocorrelation function could be described as a power law over many decades of lag time for all samples, demonstrating selfsimilarity of the gel structure. The only exception to this was for the gel with high content of α-lactalbumin which showed an oscillatory behaviour of the autocorrelation function. Significant amounts of glycosylated caseino-macro-peptide were observed in many of the samples at the position of β-lactoglobulin. However it did not affect gelation as it remains in solution.     

Effect of Two-Step Heating on Gel Properties of a Paramyosin-Myosin System

The effect of two-step Heating, including low temperature setting, on the gel properties of the paramyosin-myosin system was investigated. At relatively low paramyosin contents, little effect of the two-step heating on gel properties was observed. When the paramyosin became 25 % or more, the indices of gel properties became significantly larger than those for the gels prepared by one-step heating. Paramyosin was more susceptible to the effect of two-step heating than myosin. It was thus concluded that paramyosin was mainly responsible for the effect of setting in invertebrate muscle gels.     

高压和食盐对鸡肉肠品质特性的影响

在不同压强条件（0.1、200、400 MPa）下对不同食盐添加量（质量分数0%、1%、2%）的生鸡肉肠加热（60 ℃）处理30 min,测定处理后鸡肉肠的持水力、水分分布、质构特性和微观结构,分析高压和食盐对鸡肉肠热诱导凝胶特性的影响。结果发现：常压下,减少食盐添加量会降低鸡肉肠的保水性和质构特性,但高压处理能降低食盐对鸡肉肠的影响。相比常压组,200 MPa高压处理能显著提高产品的保水性和质构特性（P＜0.05）,而400 MPa的高压处理则显著降低产品的保水性和质构特性（P＜0.05）。高压能促进肉糜中的肌纤维分解,使不易流动水的比例升高,自由水比例下降;200 MPa下能形成致密的凝胶网络,而400 MPa则阻碍凝胶网络的形成。高压结合加热处理可用于提高低盐鸡肉肠的品质特性。     

The effects of particle size, connective tissue and cooking regime upon properties of washed mechanically recovered broiler meat

Mechanically recovered meat (MRM) from broilers was washed with water, with or without prior chopping and with or without sieving to remove connective tissue. The resultant protein extract was mixed with salt and cooked in a one-step (directly to 80°C) or two-step (to 55°C and then to 80°C) cooking regime, to form gels. Washing broiler MRM gave stronger gels with lower cooking loss and expressible moisture than unwashed broiler MRM. These washed gels were also lighter in colour and less red. The best products were produced when some of the collagen had been removed by sieving, but not if the samples had Wrst been chopped, even though the total protein and dry matter contents were also reduced. A two-step cooking procedure enhanced gel strength. Evidence of a more porous, but dense, structure of washed broiler MRM subjected to a two-step cooking treatment was given by scanning electron microscopy and these differences could be related to the changes in gel strength and water holding.     

组氨酸与氯化钾混合液对兔肉肌球蛋白特性的影响

目的：研究组氨酸与氯化钾混合液对肌球蛋白溶出率、聚集特性和热凝胶特性的影响。方法：提取纯化兔腰大肌肌球蛋白,并用含有组氨酸的盐溶液透析处理,测定不同离子强度条件下蛋白溶出率、浊度以及热诱导凝胶的硬度和保水性（water holding capacity,WHC）。结果：经组氨酸处理后,在低离子强度（1 mmol/L KCl）条件下肌球蛋白的溶出率从17.2%提高到64.4%,聚集程度显著下降,热凝胶的硬度和保水性显著提高（P＜0.05）;而在生理离子强度（0.15 mol/L KCl）和高离子强度（0.6 mol/L KCl）条件下肌球蛋白的溶出率和聚集特性均未受组氨酸处理的影响,但其热凝胶硬度值显著降低（P＜0.05）;虽然在高离子强度条件下肌球蛋白热凝胶的保水性显著降低（P＜0.05）,但是在生理离子强度条件下凝胶保水性没有发生变化。结论：组氨酸处理可以显著增强低离子强度条件下肌球蛋白溶出率和其热凝胶形成能力,是低钠凝胶类肉制品生产和研发的一个新思路。     

Thermal Gelation of Previously Cooked Minced Meat from Jonah Crab (Cancer borealis)

ABSTRACT:  Crab processing typically involves picking meat from whole cooked product. Remaining meat can be recovered as mince and potentially processed into value-added products. This study focused on gelation of commercially processed crab mince. Objectives of the research were to determine the effects of cryoprotectants, freezing, and various heat treatments on gel formation of washed mince from previously cooked crab. Previously frozen minced meat from thermally processed Jonah crab was washed to remove soluble components. Four different treatments were applied to the washed mince: (1) freezing with cryoprotectants, (2) freezing with no cryoprotectants, (3) no freezing with cryoprotectants, and (4) no freezing with no cryoprotectants. Unwashed mince was used as a control treatment. Sodium chloride (2.5%) was mixed into the mince prior to stuffing into sausage casings and heating at 35 °C/30 min, 90 °C/30 min, or 35 °C/30 min followed by 90 °C/30 min. Gels were tested for proximate composition, color, water-holding capacity, and gel strength. All mince samples formed gels except for the unwashed control. Gels with no cryoprotectants had 10% to 20% greater water holding capacity, lower L* values, and greater gel strength than those with cryoprotectants. Freezing of washed mince resulted in lower water-holding capacity of gels and higher a* values. A 2-stage heating treatment resulted in gels with the greatest gel strength, whereas gels cooked at 35 °C had the greatest distance to fracture. Results indicate that protein gels can be formed using previously cooked crab meat, which may be useful in the development of value-added products.     

Production of a high gel strength whey protein concentrate from cheese whey

In order to develop a process for the production of a whey protein concentrate (WPC) with high gel strength and water-holding capacity from cheese whey, we analyzed 10 commercially available WPC with different functional properties. Protein composition and modification were analyzed using electrophoresis, HPLC, and mass spectrometry. The analyses of the WPC revealed that the factors closely associated with gel strength and water-holding capacity were solubility and composition of the protein and the ionic environment. To maintain whey protein solubility, it is necessary to minimize heat exposure of the whey during pretreatment and processing. The presence of the caseinomacropeptide (CMP) in the WPC was found to be detrimental to gel strength and water-holding capacity. All of the commercial WPC that produced high-strength gels exhibited ionic compositions that were consistent with acidic processing to remove divalent cations with subsequent neutralization with sodium hydroxide. We have shown that ultrafiltration/diafiltration of cheese whey, adjusted to pH 2.5, through a membrane with a nominal molecular weight cut-off of 30,000 at 15 degrees C substantially reduced the level of CMP, lactose, and minerals in the whey with retention of the whey proteins. The resulting WPC formed from this process was suitable for the inclusion of sodium polyphosphate to produce superior functional properties in terms of gelation and water-holding capacity.