Heat-induced gelation of porcine blood plasma proteins as affected by pH

Porcine plasma is a by-product of the meat industry that can be used as a food ingredient. It is a protein mixture, hence its composition can be modified to meet specific functionality requirements. In the present paper, the gelation properties of plasma and its two major fractions (serum and albumin) have been studied at pH 4.5, 6.0 and 7.5. Polyacrylamide gel electrophoresis (SDS-PAGE) revealed that albumin was the constituent that remained soluble to a larger extent during heat-treatments, and that acidic coagulation occurred at pH 4.5, making weak interactions the predominating ones between protein aggregates. Differential scanning calorimetry (DSC) and rheological tests showed that both the thermal stability and the gelation point of protein solutions were lower as pH decreased. The textural properties and water-holding capacities of plasma and albumin gels were more pH-dependent than serum. Albumin gels were the weakest and those of plasma at pH 7.5, the strongest. It has been determined that interactions between protein fractions play a key role in the gelling properties due to synergistic effects. This knowledge should be useful in the engineering of a plasma derivative product designed for specific food requirements, by reformulating its natural composition and enhanced by controlling pH.     

Some specific features of the thermotropic gelation of carp actomyosin

This paper is devoted to the study of the heat treatment regime affection on the rheological properties of the actomyosin (AM) thermotropic gels of the muscle tissue of carp. It is shown, that systems containing AM undergo several conformational transitions during heating. These transitions make the essential contributions into the gelation process since they predetermine the dissociation, reassociation and aggregation of AM, i.e. they determine in the end the nature of the physicomechanical properties of the spatial network. The two- or three-staged heat treatment of the AM dispersions at narrow temperature intervals was found to be optimal in order to obtain the more elastic thermotropic 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.     

Thermal gelation of chicken, pork and hake (Merluccius merluccius, L) actomyosin

Response surface methodology compared the effects of protein concentration (PC, 5-15 mg mL(-1)), ionic strength (NaCl concentration, IS, 0.1-0.7 M) and pH (5.2-7.5) on the gelation properties (penetration test) of natural actomyosin (NAM) from chicken, pork and hake muscle. Results indicated that, for Ln work of penetration (Ln WP), models had r(2) of 0.705 (p < 0.01) for NAM from pork, 0.813 (< 0.001) for NAM from chicken and 0.264 from hake (p > 0.05). The maximum work of penetration did not differ widely among the three samples, regardless of the fact that pH, NaCl level and protein concentration were different in each case. It was found that hake NAM only formed gels within a very narrow range of PC, pH and IS compared with chicken and pork NAM. In the latter two, maximum WP levels were found in gels formed within a pH range of 5.5-6.0 and ionic strength of 0.1-0.2 (NaCl, M). This suggests that hake protein is more sensitive to changes in environmental factors than that from pork or chicken.     

Heat-induced degradation of inulin

Dry heating of inulin from chicory for up to 60 min at temperatures between 135 and 195 °C resulted in a significant degradation of the fructan ranging from 20 to 100%. The choice of the analytical method has a significant influence on inulin quantification especially in heat-treated samples. The amount of inulin found after thermal treatment measured as fructose after acidic hydrolysis was significantly higher compared with corresponding data obtained with a method based on enzymatic hydrolysis. Using high-performance anion-exchange chromatography with pulsed amperometric detection as well as high-performance thin-layer chromatography, it was found that thermal treatment of inulin leads to a degradation of the long fructose chains and formation of new products, most likely di-D-fructose dianhydrides. These degradation products of inulin are cleavable by acid to fructose monomers, but their glycosidic bonds are no longer accessible for -fructosidase, thus explaining the discrepancies in inulin quantification with respect to the method used. Inulin degradation must be taken into account when fructan is used as a prebiotic ingredient in thermally treated foods like bakery products.     

Acid-induced gelation of natural actomyosin from Atlantic cod (Gadus morhua) and burbot (Lota lota)

The acid-induced gelation of natural actomyosin (NAM) from burbot (Lota lota) and Atlantic cod (Gardus morhua) added with d-gluconic acid-δ-lactone (GDL) during incubation at room temperature (22–23 °C) for 48 h was investigated. During acidification, pH values of both NAMs reached 4.6 within 48 h. Both NAMs underwent aggregation during acidification as evidenced by increases in turbidity and particle size, especially after 6 h of incubation. The decreases in Ca²⁺-ATPase activity and salt solubility of both NAMs were observed during incubation. Decreases in total sulphydryl content with the concomitant increases in disulphide bond content of NAM from both species were also noticeable. Additionally, surface hydrophobicity of NAM increased, suggesting the conformational changes in NAM induced by acidification. The storage modulus (G′) values increased with increasing incubation time and G′ development was greater in Atlantic cod NAM, compared with burbot NAM. Differential scanning calorimetry (DSC) revealed that T_max and enthalpy of myosin peak shifted to the lower values and endothermic peak of actin completely disappeared. In general, gel development was more pronounced in Atlantic cod NAM, compared with the burbot counterpart. As visualised by transmission electron microscopy, network strands of aggregates from Atlantic cod were finer and more uniform than those of the burbot counterpart. Acid-induced gelation of NAM from both fish species therefore involved both denaturation and aggregation processes. However, gelation varied with fish species and had an impact on the resulting gels.     

血清蛋白质加热凝胶的形成

家畜血液中含有丰富的蛋白质。血液的主要成分——血清或血浆与卵白都有经加热可以形成凝胶的相同性质。食品中蛋白质凝胶的形成能力直接影响着食品的品质。通过对一定浓度的牛和猪的血清蛋白质加热形成凝胶强度的评价,分析了血清中主要蛋白质成分在凝胶形成过程中的作用及其机理。结果表明:牛血清的凝胶强度高于猪血清;牛血清中的白蛋白在血清加热凝胶形成过程中起着重要作用;通过加热血清蛋白,蛋白质分子间的二硫键交联形成凝胶;利用血清蛋白质经加热可以形成凝胶的性质将血清添加到食品中,不仅可以改善食品的品质,而且还可以提高食品中蛋白质的含量。     

Comparative study on the stability of fish actomyosin and pork actomyosin

Effects of temperature, pH and ionic strength on the stability of actomyosin (AM) from fish and pork were studied using UV spectra, solubility, turbidity, and sulfhydryl group content measurement for comparison. Pork AM exhibited higher stability to cold storage and heating than fish AM. The unfolding rate of AM increased with increasing temperature. Intense aggregation occurred over 30 °C for fish AM and 40 °C for pork AM. New disulfide bonds mainly formed over 40 °C for fish AM and 60 °C for pork AM. Pork AM exhibited the higher turbidity than fish AM in the range of 50-90 °C, suggesting the higher extent of aggregation of pork AM. Ionic strength mainly influenced solubility of AM, but there was no effect on cleavage and formation of disulfide bond. The lowest solubility of both AM was at pH 5.42. Additionally, fish AM was more sensitive to pH changes than pork AM.     

Effects of <Emphasis Type="SmallCaps">l</Emphasis>-lysine on thermal gelation properties of chicken breast actomyosin

The effects of l-lysine (l-Lys) on the water holding capacity (WHC) and texture of actomyosin (AM) gel and the possible mechanisms were investigated. l-Lys increased the WHC and hardness of the AM gel. These effects may be related to the even and continuous microstructure of the gel according to the scanning electron microscopy analysis. Furthermore, l-Lys increased the surface hydrophobic residues and the reactive sulfhydryl groups. l-Lys decreased the storage modulus at the first transition temperature but increased it at the second transition temperature and the third transition enthalpy. These results suggested that l-Lys varied the thermal behaviors and the microstructure of the AM gel by increasing the surface hydrophobicity and reactive sulfhydryl groups, ultimately contributing to the increased WHC and hardness. The changes in pH did not fully explain the results from the present study. The results were useful for understanding previous findings and may serve as a reference for the preparation of reduced-sodium and phosphate-free meat products.     

Heat-induced Gelation of Chicken Gizzard Myosin

Chicken gizzard myosin solution formed a gel when heated above 40°C. The rigidity of the gel was constant above 65°C. Maximum pH for gel formation was 5.9 at 0.6M and 5.7 at 0.15M KCl. Higher rigidity of the myosin gel was observed at low ionic strength than at high ionic strength. Rigidities of myosin at 0.6M KCl increased by (mg/mL)^2.5 and at 0.15M (mg/mL)^{1, 4} myosin concentration. The strength of gizzard myosin gels was comparable to that of myosin gels from chicken breast muscle under similar conditions.     

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.     

凝固剂及凝固条件对大豆蛋白胶凝性质的影响

以大豆蛋白的凝胶强度、持水性、凝固速率这3个胶凝特性为主要指标,测定了包括蛋白浓度、热处理温度和时间、凝固剂种类和添加量、pH值、离子强度在内的这些因素对上述胶凝性质的影响,并确定了最优凝固工艺条件:质量浓度60g/L的SPI溶液经95℃热处理15min后,分别以质量分数0.4%熟石膏(CaSO4·1/2H2O)和质量分数0.28%葡萄糖酸内酯(GDL)作为凝固剂,保温30min后,冷却至室温;最佳离子强度为0.01mol/L(NaCl)。     

Physical gelation of biopolymers

A number of topics in the area of physical gels formed from both synthetic and biological polymers are discussed. Future progress in the understanding of physical gels will be more rapid once studies of model synthetic precursors of controlled architecture begin to proliferate.     

Heat-induced changes in dairy products containing sucrose

The aim of the present work was to analyse the influence of the variables reaction temperature, casein–sucrose ratio and pH, on the kinetic parameters of gelation reactions, the gelation time and the functionality of casein micelles in concentrated milk systems containing sucrose.     

Heat-induced tenderisation of meat by endogenous carboxyl proteases

The rôle of carboxyl proteases in tenderising meat was investigated by injecting the inhibitors, pepstatin and EPNP, into pre-rigor muscle. The increase in shear force values induced by these inhibitors provided a minimum estimate of the extent to which endogenous carboxyl proteases normally tenderise meat at 60°C.Gel electrophoresis showed that connectin was hydrolysed to a greater extent than other muscle proteins at this temperature and that breakdown of connectin was inhibited by pepstatin and EPNP. Thus it is likely that, when intact, connectin may contribute to the strength of cooked meat.     

Heat-induced changes in the calcium sensitivity of caseins

The calcium sensitivity of Na caseinate prepared from a serum protein-free casein micelle dispersion in synthetic milk ultrafiltrate, containing 4.8%, w/v, lactose and 5 mmol L⁻¹ urea and heated at 130°C for 0–25 min decreased with heating. It is proposed that an increase in the net negative charge of the caseinates, due to heat-induced degradation of lysine and arginine, is responsible for the enhanced calcium stability of heated caseins. The Maillard reaction and urea–protein interactions appear to play an important role in the increased stability of heated caseinate towards calcium. The effect of protein charge on the heat stability of milk protein systems (Na caseinate 2.5%, w/v, protein in milk ultrafiltrate) at 140°C was investigated by chemical modification of the caseinate prior to assessment of heat stability. Heat stability increased with the modification of lysine, arginine and carboxyl residues. The increased heat stability of Na caseinate with modified lysine and arginine residues may be due to an increase in the net negative charge on the caseinate, while the increased stability of caseinate with modified carboxyl residues may be related to a reduction in heat-induced crosslinking of protein.     

猪肉盐溶性蛋白热诱导凝胶特性的研究

盐溶性蛋白是影响猪肉制品的保水性及凝胶特性的一类最主要蛋白质,其中对蛋白质热凝胶起决定作用的是肌球蛋白.本试验以猪肉为原料,首先通过单因素试验研究贮藏时间、离子强度、磷酸盐等因素的影响,再通过正交试验得出猪背最长肌(P1d)盐溶蛋白最合适的提取条件:MgCl2浓度0.01 mol/L、NaCl浓度0.5 mol/L、焦磷酸钠及多聚磷酸钠的比例均为0.4%.     

兔肌球蛋白热诱导凝胶过程中的物理化学变化

研究在pH6.5、高离子强度(0.6mol/L KCI)下兔肌球蛋白热诱导凝胶过程中的物理化学特性的变化.α-螺旋含量从25℃开始缓慢减小,43℃后开始急剧减小,直到65℃左右后基本不发生变化;浊度从40℃左右开始增加,表明了凝集的开始,至65℃后不再变化.活性巯基含量40℃开始增加,65℃达到最大值;总巯基含量从30℃开始降低;疏水性在30～85℃间呈非线性增加趋势;G'(贮能模量)从48℃开始增加,在48～71℃间缓慢增加,71～82℃间急剧增加.表明肌球蛋白热变性从α-螺旋的解折叠开始,进而促进疏水基团和巯基基团的暴露;二硫键与疏水作用、分子间氢键等共同作用促进凝胶强度的增加.     

牛肉盐溶蛋白质热诱导凝胶特性研究

实验以牛背最长肌为材料,采用L9（3^4）正交设计研究了MgCl2、NaCl和pH值对盐溶蛋白质热诱导凝胶特性的影响。研究表明,在0．01mol／LMgCh．0．6mol／LNaCl．pH值7．0条件下牛背最长肌盐溶蛋白质热诱导凝胶保水性最好,为92．25％,破断应力最高,为14．00kPa。NaCl浓度和pH值对凝胶保水性和凝胶强度均有显著影响（p〈0．01）。MgCl12仅对凝胶破断应力影响较大。凝胶的超微结构分析表明,保水性高的凝胶的网络结构比较致密,大量的微细孔洞均匀分布。保水性低的凝胶的网络结构中线条多呈束状、结构粗糙、不均匀。     

Heat-induced Egg White Gels as Affected by pH

The functional properties of heat-induced egg white gels were investigated at five pH values. Textural characteristics were determined using the Instron Universal Machine. Hardness, elasticity, cohesiveness, chewiness, and fracturability were maximum at pH 11. Hunter L values were maximum at pH 5 and 7. Microstructure studied with electron microscopy was distinctly different at the five pH values. Alkaline gels showed a fine ordered network that might have contributed to excellent textural characteristics. Water-holding capacity (WHC) was high at alkaline pH, but decreased with addition of 2-mercaptoethanol, suggesting that disulfide bonds were important in egg white gels. Sodium dodecyl sulfate (SDS) improved WHC at pH 7 and 9. No significant correlation was observed between textural profiles and WHC.