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1.
Physicochemical changes of myosin during heating were investigated to elucidate the mechanism of heat-induced gelation of arrowtooth flounder (ATF) myosin at high ionic strength. Changes in dynamic properties indicated ATF myosin formed a gel in three different stages as shown by the first increase in G' (storage modulus) at 28 degrees C, followed by the decrease at 35 degrees C and the second increase at 42 degrees C. DSC thermogram showed the onset of myosin denaturation at 25 degrees C with two maximum transition temperatures at 30 and 36 degrees C. The decrease in alpha-helical content indicated ATF myosin began to unfold at 15 degrees C and the unfolding continued until it reached 65 degrees C. Turbidity measurement showed myosin began to aggregate at 23 degrees C and the aggregation was complete at 40 degrees C. Surface hydrophobicity increased consistently in the temperature range studied, 20-65 degrees C. Sulfhydryl contents decreased significantly at 20-30 degrees C due to the formation of disulfide linkages but remained constant at temperatures >30 degrees C. ATF myosin was shown to be extremely sensitive to heat, resulting in denaturation at lower temperature than other fish myosin. Denaturation was initiated by unfolding of the alpha-helical region in myosin followed by exposure of hydrophobic and sulfhydryl residues, which are subsequently involved in aggregation and gelation processes.  相似文献   

2.
Thermal, rheological, and microstructural properties of myosin (1 and 2% protein) were compared to mixtures of 1% myosin and 1% heat-denatured beta-lactoglobulin aggregates (myosin/HDLG) and 1% myosin and 1% native beta-lactoglobulin (myosin/beta-LG) in 0.6 M NaCl and 0.05 M sodium phosphate buffer, pH 6.0, 6.5, and 7.0 during heating to 71 degrees C. Thermal denaturation patterns of myosin and myosin/HDLG were similar except for the appearance of an endothermic peak at 54-56 degrees C in the mixed system. At pH 7.0, 2% myosin began to gel at 48 degrees C and had a storage modulus (G') of 500 Pa upon cooling. Myosin/HDLG (2% total protein) had a gel point of 48 degrees C and a G' of 650 Pa, whereas myosin/beta-LG had a gel point of 49 degrees C but the G' was lower (180 Pa). As the pH was decreased, the gel points of myosin and myosin/HDLG decreased and the G' after cooling increased. The HDLG was incorporated within the myosin gel network, whereas beta-LG remained soluble.  相似文献   

3.
The denaturation, aggregation, and rheological properties of chicken breast muscle myosin, beta-lactoglobulin (beta-LG), and mixed myosin/beta-LG solutions were studied in 0.6 M NaCl, 0.05 mM sodium phosphate buffer, pH 7.0, during heating. The endotherm of a mixture of myosin and beta-LG was identical to that expected if the endotherm of each protein was overlaid on the same axis. The maximum aggregation rate (AR(max)) increased, and the temperature at the AR(max) (T(max)) and initial aggregation temperature (T(o)) decreased as the concentration of both proteins was increased. The aggregation profile of <0.5% myosin was altered by the presence of 0.25% beta-LG. Addition of 0.5-3.0% beta-LG decreased storage moduli of 1% myosin between 55 and 75 degrees C, but increased storage moduli (G') when heated to 90 degrees C and after cooling. beta-LG had no effect on the gel point of > or =1.0% myosin, but enhanced gel strength when heated to 90 degrees C and after cooling. After cooling, the G' of 1% myosin/2%beta-LG gels was about 1.7 times greater than that of gels prepared from 2% myosin/1% beta-LG.  相似文献   

4.
Changes in the conformation of catfish (Ictalurus punctatus) myosin due to (i) anions, (ii) acid pH, and (iii) salt addition were determined using tryptophan fluorescence, hydrophobicity measurements, differential scanning calorimetry, and circular dichroism. The relationship between conformation and storage modulus (G') of acid-treated myosin was studied. Three acids, HCl, H2SO4, and H3PO4, were used for unfolding myosin at three acidic pH conditions, 1.5, 2.0, and 2.5. Unfolded myosin was refolded to pH 7.3. Denaturation and unfolding of myosin was significantly (p < 0.05) lower when salt (0.6 M NaCl) was present during acid unfolding than in the absence of salt. When salt was added before unfolding, the alpha-helix content of myosin treated at pH 1.5 was significantly lower than that treated at pH 2.5. When salt was added after refolding, the alpha-helix content of myosin was unaffected by different pH treatments. The G' of myosin increased with an increase in myosin denaturation. The G' of myosin was significantly (p < 0.05) higher when salt was added to myosin after refolding than before acid unfolding. Among the different anion treatments, the G' of acid-treated myosin decreased in the order Cl- approximately SO42- > PO43-. Among the different pH treatments, the G' of myosin treated at pH 1.5 was significantly (p < 0.05) higher than myosin treated at pH 2.5. The conditions that would result in maximum myosin denaturation and maximum G' were unfolding of myosin at pH 1.5 using Cl- (from HCl) followed by refolding at pH 7.3 and subsequent addition of 0.6 M NaCl.  相似文献   

5.
The effects of Trichoderma reesei tyrosinase-catalyzed cross-linking of isolated chicken breast myofibril proteins as a simplified model system were studied with special emphasis on the thermal stability and gel formation of myofibrillar proteins. In addition, tyrosinase-catalyzed cross-linking was utilized to modify the firmness, water-holding capacity (WHC), and microstructure of cooked chicken breast meat homogenate gels. According to SDS-PAGE, the myosin heavy chain (MHC) and troponin T were the most sensitive proteins to the action of tyrosinase, whereas actin was not affected to the same extent. Calorimetric enthalpy (DeltaH) of the major thermal transition associated with myosin denaturation was reduced and with actin denaturation increased in the presence of tyrosinase. Low-amplitude viscoelastic measurements at constant temperatures of 25 degrees C and 40 degrees C showed that tyrosinase substantially increased the storage modulus (G') of the 4% myofibrillar protein suspension in the 0.35 M NaCl concentration. The effect was the most pronounced with high-enzyme dosages and at 40 degrees C. Without tyrosinase, the G' increase was low. Tyrosinase increased the firmness of the cooked phosphate-free and low-meat chicken breast meat homogenate gels compared to the corresponding controls. Tyrosinase maintained gel firmness at the control level of the low-salt homogenate gel and weakened it when both salt and phosphate levels were low. Tyrosinase improved the WHC of the low-meat and low-salt homogenate gels and maintained it at the level of the corresponding controls of phosphate-free and low-salt/low-phosphate homogenate gels. Microstructural characterization showed that a collagen network was formed in the presence of tyrosinase. Keywords: Chicken myofibrillar proteins; protein modification; cross-linking; tyrosinase; gelation; thermal stability; texture; water-holding capacity; microstructure.  相似文献   

6.
Heat-induced gel formation by soy proteins at neutral pH   总被引：9，自引：0，他引：9  
Heat-induced gel formation by soy protein isolate at pH 7 is discussed. Different heating and cooling rates, heating times, and heating temperatures were used to elucidate the various processes that occur and to study the relative role of covalent and noncovalent protein interactions therein. Gel formation was followed by dynamic rheological measurements. Heat denaturation was a prerequisite for gel formation. The gelation temperature (84 degrees C) was just above the onset denaturation temperature of glycinin. The stiffness of the gels, measured as the elastic modulus, G', increased with the proportion of denatured protein. An increase in G' was also observed during prolonged heating at 90 degrees C. This increase is explained by the occurrence of rearrangements in the network structure and probably also by further incorporation of protein in the network. The increase in G' upon cooling was thermoreversible indicating that disulfide bond formation and rearrangements do not occur upon cooling.  相似文献   

7.
The effect of laccase and transglutaminase (TG) on cross-linking, gelation, and thermal stability of salt-soluble chicken-breast myofibril proteins was investigated at pH 6. Both enzymes modified the protein pattern detected by SDS-PAGE. Identification of proteins by peptide mass mapping showed that myosin heavy chain (MHC) and troponin T were the most affected proteins. These proteins faded or disappeared as a function of the incubation time with both enzymes on SDS-PAGE. The molecular weight of actin was not, however, affected by either enzyme. The effects that the enzymes had on the gel formation of chicken-breast myofibrils were studied in 0.35 and 0.60 M NaCl solutions at 3% protein content and a constant temperature of 40 degrees C by using a small deformation viscoelastic measurement. TG substantially increased the storage modulus (G') of 3% protein in 0.35 M NaCl. Without the enzymes, gelation was insignificant in 0.35 M NaCl. The increased solubility of the proteins at 0.60 M NaCl intensified gelation with TG. G' increased 32 and 64% at dosages of 10 and 100 nkat of TG, respectively. Also, laccase increased G' of the gel in 0.60 M salt concentration. However, a high laccase dosage decreased the magnitude of G' below the control level. Differential scanning calorimetric (DSC) measurements indicated slightly reduced myosin heat stability after TG pretreatment and increased actin heat stability with both enzymes. Maximum transition temperatures did not alter with either enzyme.  相似文献   

8.
Thermal denaturation, rheological, and microstructural properties of gels prepared from native beta-lactoglobulin (beta-LG) and preheated or heat-denatured beta-LG (HDLG) aggregates were compared. The HDLG was prepared by heating solutions of 4% beta-LG in deionized water, pH 7.0, at 80 degrees C for 30 min and then diluted to the desired concentration in 0.6 M NaCl and 0.05 M phosphate buffer at pH 6.0, 6.5, and 7.0. When reheated to 71 degrees C, HDLG formed a gel at a concentration of 2% protein. At pH 7.0, 3% HDLG gelled at 52.5 degrees C and had a storage modulus (G') of 2200 Pa after cooling. beta-LG (3%) in 0.6 M NaCl and 0.05 M phosphate buffer, pH 7.0, did not gel when heated to 71 degrees C. The gel point of 3% HDLG decreased by 10.5 degrees C and the G' did not change when the pH was decreased to 6.0. The HDLG gel microstructure was composed of strands and clumps of small globular aggregates in contrast to beta-LG gels, which contained a particulate network of compacted globules. The HDLG formed a gel at a lower concentration and lower temperature than beta-LG in the high-salt buffer, suggesting an application in meat systems or other food products prepared with salt and processed at temperatures of < or =71 degrees C.  相似文献   

9.
Myosin rod and light meromyosin (LMM) of walleye pollack and white croaker were examined for their rheological properties by measuring dynamic viscoelastic parameters. Rods from walleye pollack and white croaker increased their storage moduli (G') in the ranges of 29-43 degrees C and 31-38 degrees C, respectively, in temperature sweep analysis. Walleye pollack LMM showed no peak of G' upon heating, whereas the white croaker counterpart exhibited a single sharp peak of G' at 35 degrees C. Loss modulus (G") showed similar temperature-dependent changes for the two fish species as the case of G', irrespective of rod and LMM, although G" values were lower than those of G'. Thus, rheological properties of rod and LMM were different between walleye pollack and white croaker. Taken together with data previously reported for myosin, it was considered that both myosin rods from walleye pollack and white croaker are attributed to thermal gel formation of myosin in a low-temperature range, though in a species-specific manner.  相似文献   

10.
This study demonstrated that the novel isoelectric solubilization/precipitation can be applied to recover functional muscle protein in a continuous mode from whole Antarctic krill. Protein recovered from whole krill had a much lower ash content than whole krill, suggesting good removal of inedible impurities (shell, appendages, etc.). Lipids were retained to a higher degree with krill protein solubilized at acidic rather than basic pH. The viscoelastic modulus (G') showed that recovered krill protein failed to form heat-induced gel unless beef plasma protein (BPP) was added. Therefore, protease inhibitors are suggested for development of krill-derived products. Even with BPP, the G' decreased between 45 and 55 degrees C. However, krill protein solubilized at acidic pH had a higher decrease of the G' than the protein solubilized at basic pH, likely due to krill endogenous cathepsin L. Krill protein-based gels developed from protein solubilized at basic pH, especially pH 12.0, had better texture (torsion and Kramer tests and texture profile analysis) than acidic counterparts, possibly due to higher proteolysis and denaturation at acidic pH. Gels made from protein solubilized at acidic pH were brighter and whiter likely due to a higher lipid content.  相似文献   

11.
为探究漂洗和斩拌对海鲈鱼肌球蛋白理化特性的影响,分别提取原料、漂洗鱼糜、斩拌鱼糜的肌球蛋白,通过测定总巯基、活性巯基、表面疏水性、浊度等基本性质,并结合红外光谱和原子力显微镜(atomic force microscope,AFM)技术对肌球蛋白二级结构和表面形貌进行研究。结果表明:相比原料,漂洗鱼糜肌球蛋白总巯基含量降低19.5%,活性巯基增大63.9%,而斩拌鱼糜肌球蛋白总巯基和活性巯基的质量分数相比漂洗鱼糜分别降低22.6%和66.8%,漂洗鱼糜的肌球蛋白变性程度最大;肌球蛋白浊度和表面疏水性在经过漂洗和斩拌均增大,漂洗对表面疏水性影响更大,斩拌对浊度影响更大;红外光谱研究结果显示,漂洗对二级结构影响更明显,原料经过漂洗后,α-螺旋相对含量降低了33.16%,无规则卷曲相对含量增加了79.42%,β-折叠和β-转角分别增加1.11%和10.38%,斩拌后,鱼糜肌球蛋白二级结构变化率较低;漂洗和斩拌都可改变肌球蛋白的表面形貌,使肌球蛋白聚集簇明显减小,聚集高度增加。研究结果证明,漂洗和斩拌对肌球蛋白理化特性有很大的影响,是鱼糜具有更好的凝胶性能的重要步骤。  相似文献   

12.
The heat-induced denaturation curve of ovalbumin followed by the ellipticity at 222 nm in circular dichroism spectra was consistent with that monitored by fluorescence with thioflavin T, which is an indication of amyloid fibril formation, while other proteins such as lysozyme and ovotransferrin did not fluoresce with thioflavin T during heat denaturation. The amount of soluble aggregate formed during heat denaturation was proportional to the increase in fluorescence with thioflavin T. The binding of soluble aggregates with thioflavin T was greatly suppressed in heat-denatured ovalbumin in the presence of thioflavin T. The similar inhibition effect of thioflavin T on the gel formation of heat-induced ovalbumin was observed. These results suggest that the amyloidogenic intermolecular beta-structure is involved in the formation of soluble aggregate and gel of heat-induced ovalbumin.  相似文献   

13.
The starches were separated from unripe apples of five cultivars (Criterion, Ruspippum, Red Spur, Skyline Supreme, and Granny Smith) and evaluated using scanning electron microscopy (SEM), gel permeation chromatography (GPC), X-ray diffraction, differential scanning calorimetry (DSC), and dynamic viscoelasticity. SEM showed the presence of round granules as well as granules that had been partially degraded, probably by amylases. The starch granules in different apple starches ranged between 4.1 and 12.0 mum. Debranching of starch with isoamylase and subsequent fractionation of debranched materials by GPC revealed the presence of an apparent amylose, an intermediate fraction (mixture of amylose and amylopectin), long side chains of amylopectin, and short side chains of amylopectin in the range of 28-35.2, 3.6-4.4, 20-21.3, and 39.9-47.1%, respectively. The swelling power of starches ranged between 14.4 and 21.3 g/g. X-ray diffraction of apple starches showed a mixture of A- and B-type patterns. All apple starches showed peak intensities lower than that observed for normal corn and potato starch, indicating the lower crystallinity. The transition temperatures (onset temperature, T(o); peak temperature, T(p); and conclusion temperature, T(c)) and enthalpy of gelatinization (deltaH(gel)) determined using DSC ranged between 54.7 and 56.2 degrees C, between 57.1 and 59.1 degrees C, between 60.2 and 63.5 degrees C, and between 3.3 and 4.2 J/g, respectively. The viscoelastic properties of starch from different cultivars measured during heating and cooling using a rheometer differed significantly. Red Spur and Criterion starches with larger granule size showed higher G' and G' ' values, whereas those containing smaller size and amylolytically degraded granules showed lower G' and G' '.  相似文献   

14.
Thermal denaturation and aggregation abilities of salmon myofibrils and myosin were studied measuring turbidity, intrinsic fluorescence, 8-anilino-1-naphthalene sulfonic acid binding, and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide cross-linking. The thermal behaviors of protein preparation from white and red muscles were compared, and the relationship with thermal gelation properties is discussed. The low gelation ability of salmon muscle proteins was related to a limited extent of protein denaturation and aggregation upon heating. These properties seemed to be carried by myosin molecules as a similar behavior was observed for both myofibrils and myosin preparations. The higher thermal stability observed for red muscle proteins with higher transition temperatures in rheological profiles was related to a shift to higher temperature in denaturation and aggregation processes. The extent of denaturation and aggregation was very similar for both muscle types as was the final rigidity of the gels formed.  相似文献   

15.
The rheological properties of kappa-carrageenan helices dispersed in an aqueous medium, which prevents aggregation of helices, were investigated. A dispersion of 1.5% w/w nonaggregated kappa-carrageenan helices exhibited gel-like dynamic mechanical spectra at 20 degrees C; that is, the storage modulus G' predominated over the loss modulus G' ' in the entire frequency range examined (0.5-100 rad/s). However, the observed slight frequency dependence of the moduli and the relatively large value of tan delta (= G' '/G' > 0.1) were typical of so-called weak gels. The magnitude of G' of the kappa-carrageenan weak gels was less than that of conventional gels formed by 0.15% w/w kappa-carrageenan in an aggregating condition at 20 degrees C. Under large deformation, enough for the conventional gels to rupture, the weak gel systems flowed but never ruptured, suggesting that the weak gel-type rheological properties of the kappa-carrageenan dispersions were due to a sufficiently long relaxation time of topological entanglements among double-helical conformers but not due to the formation of a three-dimensionally percolated permanent network.  相似文献   

16.
The behavior of β-lactoglobulin (β-Lg) during heat treatments depends on the environmental conditions. The influence of the presence or absence of a reducing sugar, namely, glucose, on the modification of the protein during heating has been studied using fluorescence, polyacrylamide gel electrophoresis (PAGE), size-exclusion chromatography (SEC), and transmission electron microscopy. Glycated products were formed during heating 24 h at 90 °C and pH 7. The fluorescence results revealed an accumulation of the advanced Maillard products and the formation of aggregates during heating. PAGE and SEC data suggested that the products in the control samples were essentially composed of covalently linked fibrillar aggregates and that their formation was faster than that for glycated samples. We showed that glucose affected the growing step of covalent aggregates but not the initial denaturation/aggregation step of native protein. Glucose-modified proteins formed a mixture of short fibrils and polydisperse aggregates. Our results revealed that β-Lg forms fibrils at neutral pH after heating and that glucose slows the formation of these fibrils.  相似文献   

17.
The aggregation behavior during heating of a solution containing soy protein and whey protein isolate (WPI) was studied using rheology, confocal microscopy, gel filtration, and electrophoresis. Soy/WPI mixtures formed gels at 6% total protein concentration with a high elastic modulus (G') and no apparent phase separation. The ratio of soy to WPI was fundamental in determining the type of network formed. Systems containing a high soy to WPI ratio (>70% soy protein) showed a different evolution of the elastic modulus during heat treatment, with two apparent stages of network development. Whey proteins formed disulfide bridges with soy proteins during heating, and at low ratios of soy/WPI, the aggregates seemed to be predominantly formed by 7S, the basic subunits of 11S and beta-lactoglobulin. Size exclusion chromatography indicated the presence of high molecular weight soluble complexes in mixtures containing high soy/WPI ratios. Results presented are the first evidence of interactions between soy proteins and whey proteins and show the potential for the creation of a new group of functional ingredients.  相似文献   

18.
Natural fermentation of whole polished rice grains (indica) is a traditional processing method widely applied in China and South Asia to improve the texture of rice noodles. To elucidate the effects of fermentation on noodle texture, thermal analysis of rice flour and rheological measurement were performed on a gel made from the rice flour with the same solids concentration as practical noodles. The test method proved useful for monitoring starch granule swelling, gel forming, and retrogradation of rice gels during rice noodle production. Dynamic viscoelasticity in a temperature ramp sweep test showed that starch granules of the fermented sample swelled more and were more resistant to breakdown than those of the nonfermented sample. Differential scanning calorimetry revealed that the gelatinization temperature of fermented rice flour shifted to a lower temperature. The decreased protein content after fermentation also played a role in the modified rheological and thermal properties of fermented rice flour. Both fermented and nonfermented rice flour formed an elastic gel just after heating to the conclusion temperature of gelatinization (Tc). The fermented rice flour gel formed earlier with a well‐formed structure; however, it had slower retrogradation during aging. The result also indicated that the retrogradation of amylopectin impaired the desired texture of rice noodles.  相似文献   

19.
We present the results of a Fourier transform infrared (FT-IR) microspectroscopic study using conventional FT-IR microscopy and FT-IR imaging to detect the denaturation process during four different heating temperatures (raw, 45, 60, and 70 degrees C) spatially resolved in bovine cryosections from longissimus dorsi muscle. FT-IR imaging, employing a focal plane array detector, which allowed the simultaneous collection of spectra at 4096 pixels, enabled the investigation of the heat-induced changes in the two major meat constituents, i.e., myofibrillar and connective tissue proteins, spatially resolved. The infrared spectra of both compounds revealed that the major spectral changes involved an increase in beta-sheet and a decrease in alpha-helical structures, which appeared to be much more pronounced for the myofibers than for the connective tissue. These conformational changes could be correlated to the denaturation of the major meat proteins, such as myosin, actin, and collagen.  相似文献   

20.
Natural actomyosin (NAM) extracted in 0.6 M NaCl from hake fillets stored at -20 and -30 degrees C for up to 49 weeks was studied. The extracted protein decreased as storage progressed and became poorer in myosin while the proportion of actin remained constant. Two major peaks composed of myosin plus actin and actin plus tropomyosin plus troponins were obtained by size exclusion chromatography. SDS-PAGE analysis of the protein retained in the precolumn filter showed that there was protein aggregated by covalent bonding. Surface hydrophobicity increased while Ca(2+)-ATPase activity, apparent viscosity, and SH groups decreased as storage progressed. The loss of Ca(2+)-ATPase activity was due mainly to denaturation of the extracted myosin, whereas the minimum viscosity values occurred earlier and were not directly due to the lower proportion of myosin in the extracts. Thus, the extracted NAM exhibited changes during frozen storage. The temperature-dependent difference was mainly quantitative due to a smaller amount of protein extracted at -20 degrees C.  相似文献   

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