Effect of temperature and concentration on rheological behavior of xanthan-carob mixed gels

The gelation and melting behavior of 1∶1, 1∶3 xanthan-carob mixed gels were evaluated at isothermal and non-isothermal states, as a function of total polymer concentrations of 0.1, 0.5 and 1%. A thermal hysteresis was observed between gelation and melting. The higher the polymer concentration, the higher the melting temperature. The gelation points were determined by three criteria. Depending on the criterion used the gelation temperature was different (52 to 70°C). Pseudoequilibrium modulus and elastic active network chain (EANC) concentration were calculated from the plateau modulus in the frequency spectrum. Temperature dependence of the monomeric friction coefficient was estimated from the relaxation time and EANC. Time-temperature superposition theory was not applicable due to dramatic phase transitions occurring during the gelation of X/C mixture.     

Effect of surfactants on the thermal, conformational and rheological properties of collagen

Collagen is an important biomaterial and its interaction with surfactant is important in light of its use in various cosmetics and dermatological applications. Presently, the effect of surfactants on the physico-chemical properties of collagen has been studied. The thermal stability of collagen is reduced by sodium dodecyl sulfate and hexadecyltrimethylammmonium bromide, whereas Triton X-100 does not. The viscosity of collagen is influenced greatly depending on the surfactant concentrations. The secondary structure of collagen shows changes only in the molar ellipticity. The role of charge and concentration of surfactants in influencing the various physico-chemical properties of collagen has been elucidated.     

Influence of temperature on the rheological behavior of a new fucose-containing bacterial exopolysaccharide

The effect of temperature on the rheology of a new fucose-containing extracellular polysaccharide (EPS) was evaluated. The steady state data revealed a shear-thinning behavior, with the viscosity being immediately recovered when the shear rate was decreased. The mechanical spectra indicated viscous solutions with entangled polymer molecules in the range of temperatures studied (from 15 °C to 65 °C). In addition, the Time-Temperature Superposition principle was successfully applied and the Cox-Merz rule was valid, reinforcing the idea of a thermorheologically simple behavior for the EPS in aqueous solution. Furthermore, the viscous and viscoelastic properties at 25 °C were maintained after consecutive heating and cooling cycles, indicating a good thermal stability under temperature fluctuations.     

Chain conformation and rheological behavior of an extracellular heteropolysaccharide Erwinia gum in aqueous solution

The chain conformation of a heteropolysaccharide Erwinia gum (EG) consisting of Glc, Gal, Fuc, and GlcA in aqueous solution was investigated by using viscometry and static and dynamic light scattering. The Huggins constants k′ ranging from 0.31 to 0.35, and the larger second virial coefficient A₂ of the order of 10⁻⁴ and even 10⁻³ mol g⁻² cm³ for EG fractions having different molecular weights in 0.03 M NaCl aqueous solution at 25 °C, suggested that 0.03 M NaCl aqueous solution is a good solvent for EG polysaccharide. Smidsrød’s ‘B-value’ characterizing chain stiffness was estimated to be 0.028-0.045 for EG fractions indicating that the backbone of EG polysaccharide is semi-stiff having similar stiffness to the semi-stiff Alginate and CMC. The hydrodynamic factor ρ (1.69-1.89), Flory-Fox factor Φ, and the product of ρΦ/N_A (0.16-0.22) also confirmed the semi-stiffness of EG polysaccharide chains. Compared with general flexible polymers, the first remarkable shear-thinning and then Newtonian flowing behaviors in steady shear tests for EG polysaccharides were ascribed to the alignment of extended semi-stiff chains on shearing. The dynamic oscillatory shear experiments indicated that addition of certain amount of NaCl effectively prohibited its gelation in pure water even at high concentration and low temperature for long time, suggesting that 0.03 M NaCl aqueous solution of EG has good stability and ability of antigelation, and thus is a promising additive in food field.     

Effect of pH on the ternary solution behavior of beta-lactoglobulin

Ternary phase diagrams (TPDs) were constructed for aqueous beta-lactoglobulin solutions containing ethanol and (NH4)2SO4 at pHs of 7, 5, and 3 for temperatures between 20 and 70 degrees C. The addition of (NH4)2SO4 generally led to the production of a reversible precipitate, a transformation that was not strongly influenced by temperature or pH. In contrast, at pH 7 and 20 degrees C, ethanol concentrations >12% led to the formation of a molten-globule structure, which gelled at protein concentrations >10%. Destabilization of beta-lactoglobulin structure occurred at lower ethanol concentrations as temperature was increased, until at 70 degrees C, all solutions that were previously liquid at room temperature had transformed into a gel. At pH 5.0, near beta-lactoglobulin's isoelectric point, demixing dominated, leading to the creation of either irreversible precipitates or a paste-like microgel. Elevated temperatures caused the previously liquid morphology to transform into either a reversible aggregate or microgel. Solution behavior at pH 3 had characteristics of what was observed at pHs 7 and 5. At moderated protein and ethanol concentrations, a paste-like microgel was observed, whereas at higher ethanol concentrations, beta-lactoglobulin formed a gel. This work demonstrates how small changes in protein structure at the molecular level can have a dramatic effect on macroscopic morphology.     

Effect of ATP concentration and temperature on firefly luciferase activity

The dependence of luciferase activity in the homogenate of leaves of transgenic tobacco plants with chimeric firefly luciferase gene on ATP concentration and temperature was studied. The optimum ATP concentration was between 0.625 mM and 2.5 mM. The activity rapidly decreased if the homogenate was kept in 25°C and is completely lost during 30 min.     

Effect of salt concentration and temperature on survival of Legionella pneumophila

The effects of various concentrations of sodium chloride solutions (0·1%–3%) and different temperatures (4, 10, 20, 30 and 37 °C) on survival of Legionella pneumophila were investigated. It was found that at temperatures between 4 °C and 20 °C, Legionella organisms survived in salt solutions up to 3% NaCl. Only the combination of high temperatures, i. e. 30 °C and 37 °C, with NaCl concentrations over 1·5%, reduced cell numbers significantly. It was interesting to note that the addition of small amounts of NaCl (0·1%–0·5%) enhanced survival of Leg. pneumophila , suggesting a protective effect of NaCl. In order to obtain information about conditions encountered in the environment, the survival experiments were repeated in sterile sea water from the Baltic Sea and the North Sea. The marked bacterial die-off, especially at higher temperatures, was not observed in natural sea water. All these results indicate that Leg. pneumophila can survive in the marine environment.     

温度对大猿叶虫Colaphellus bowringi Baly交配行为的影响

为了探明温度对大猿叶虫Colaphellus bowringi Baly的交配行为的影响,在光周期LD 12:12,温度22℃,25℃和28℃下,观察了该虫的交配节律、日交配频率、交配持续时间和每日总交配时间.结果表明,该虫的交配节律受温度的影响,22℃下的交配高峰(上午9:00)较25℃和28℃下的交配高峰(上午8:00)推迟了1 h.温度对日交配频率和交配持续时间也有明显影响,22℃下日交配频率显著低于25℃和28℃,而交配持续时间则显著长于25℃和28℃.该虫每日总交配时间在这3种温度下变化不明显,而在较低温度下日交配频率的下降可能是由于交配持续时间延长所致.     

The thermal behavior of collagen in solution: effect of glycerol and 2-propanol

The thermal stability of different solutions of collagen (Col), collagen mixed with glycerol (Col-G) and collagen mixed with 2-propanol (Col-P) was studied by differential scanning calorimetry (DSC), viscosity and fluorescence. The DSC and viscosity methods showed that glycerol increased the denaturation temperature of collagen about 2°C, while 2-propanol decreased it about 2°C. The values of intrinsic viscosity ([η]) for Col, Col-G and Col-P were 21.67, 20.20 and 24.71 dl/g, respectively. Huggins coefficient (k(H)) increased in the presence of glycerol and decreased in the presence of 2-propanol. It was suggested that glycerol promoted the dissolution of collagen molecular aggregates while 2-propanol enhanced the aggregation. Fluorescence spectra were investigated within the temperature ranging from 15 to 45°C. By comparing the sign of peaks in the two-dimensional (2D) fluorescence correlation maps, the orders of peak response were ～360, ～410>297 nm for Col and Col-G, and 297>～360, ～410 nm for Col-P, respectively. These indicated that the respondences of tyrosine residues, excimer-like species and bityrosine on the perturbation of temperature were different in the presence of glycerol and 2-propanol.     

Quantification of human neutrophil motility in three-dimensional collagen gels. Effect of collagen concentration.

Leukocytes must migrate through tissues to fulfill their role in the immune response, but direct methods for observing and quantifying cell motility have mostly been limited to migration on two-dimensional surfaces. We have now developed methods for examining neutrophil movement in a three-dimensional gel containing 0.1 to 0.7 mg/ml rat tail tendon collagen. Neutrophil-populated collagen gels were formed within flat glass capillary tubes, permitting direct observation with light microscopy. By following the tracks of individual cells over a 13.5-min observation period and comparing them to a stochastic model of cell movement, we quantified cell speed within a given gel by estimating a random motility coefficient (mu) and persistence time (P). The random motility coefficient changed significantly with collagen concentration in the gel, varying from 1.6 to 13.3 x 10(-9) cm2/s, with the maximum occurring at a collagen gel concentration of 0.3 mg/ml. The methods described may be useful for studying tissue dynamics and for evaluating the mechanism of cell movement in three-dimensional gels of extracellular matrix (ECM) molecules.     

The effect of synthesis temperature on the rheological properties of native dextran

Summary We observed that, by varying the synthesis temperature of native dextrans, their rheological behaviors in steady state as well as in transient experiments, were substantially changed. We have also shown that the degree of branching of the dextran molecules increases with synthesis temperature. Thus, we anticipate the possibility of controlling the rheological properties of dextran through the conditions of synthesis reactions.     

Observations on the different substrate behavior of tropocollagen molecules in solution and intermolecularly cross-linked tropocollagen within insoluble polymeric collagen fibrils.

Bacterial collagenase was used to compare the extent of digestion of tropocollagen monomers in solution and in reconstituted fibrils with that of tropocollagen molecules intermolecularly cross-linked within insoluble polymeric collagen fibrils obtained from mature tendons at given time-intervals. The extent of digestion of tropocollagen monomers in solution was directly proportional to the enzyme concentration (a range of enzyme substrate molar ratios 1:200 to 1:10 was used). The extent of digestion of polymeric collagen was followed by measuring the solubilization of fluorescent peptides from fluorescent-labelled insoluble polymeric collagen fibrils. The extent of digestion of tropocollagen within polymeric collagen was linear over a very small range of enzyme concentrations, when the enzyme/substrate ratio in the reaction mixture was less than 1:400 on a molecular basis. The behavior of tropocollagen in the form of reconstituted collagen fibrils, which had been matured at 37 degrees C for 8 weeks, was intermediate between the behaviour of solutions of tropocollagen and insoluble polymeric collagen fibrils. The significance of the results is discussed in terms of the structure of polymeric collagen fibrils and the protection against enzymic attack provided by tropocollagen molecules on the circumference of the fibril. The results suggest that assays of collagenase activities based on tropocollagen as substrate cannot be directly related to the ability of these enzymes to degrade mature insoluble collagen fibrils.     

The effect of temperature and salt concentration on the circular dichroism exhibited by unionized derivatives of L-alanine in aqueous solution

The circular dichroism of Ac–Ala–NHMe, cyclo(–Ala–Ala–), Ac–Ala–OMe, Ac–Ala–Ala–OMe, and Ac–Ala–Ala–Ala–OMe has been measured in water and in aqueous salt solutions as a function of temperature. Only cyclo(–Ala–Ala–) exhibits circular dichroism which is independent of temperature. Each of the linear derivatives of L -alanine exhibits a positive circular dichroism in the range 208–218 nm at 15°C in water. Heating reduces the intensity of the positive circular dichroism, and only Ac–Ala–OMe retains positive circular dichroism at 75°C in water. Isothermal addition of salts produces changes in the circular dichroism of linear derivatives of L -alanine which resemble those seen on heating. The relative effectiveness of the salts tested, at a concentration of 4M, is LiCl ? KCl = NaCl < MgCl₂ ? CaCl₂ ? NaClO₄. The circular dichroism of cyclo(–Ala–Ala–) is also affected by the salts. Extrapolation of the results obtained with Ac–Ala–OMe, Ac–Ala–Ala–OMe, and Ac–Ala–Ala–Ala–OMe to a long polypeptide with a –CH₂R side chain in the L -configuration leads to the conclusion that this polypeptide should exhibit a temperature-dependent salt-sensitive positive circular dichroism between 208 and 218 nm when it exists as a statstical coil.     

Comparative rheological behavior of hyaluronan from bacterial and animal sources with cross-linked hyaluronan (hylan) in aqueous solution

Using a variety of rheological techniques, the behavior of hyaluronan (M(w) 0.8-2.2 x 10(6)), cross-linked hyaluronan (hylan) (M(w) 1.8-12.5 x 10(6)), and Healon (M(w) approximately 5 x 10(6)) (a proprietary hyaluronan) was studied over a large range of molecular weights. The object was to study the effect of the cross-links in hylan on the various rheological parameters, in comparison with linear hyaluronan. There are significant differences. The Huggins constant and the critical overlap parameter C*[eta] are considerably lower for hylan and an increase in moduli at low frequencies was observed for hylan compared with the hyaluronan samples at all molecular weights studied. The results point to a difference in structure in dilute solution for hylan due to the ability to form networks, which can be removed by pressure filtration. In contrast, we do not find an increase of the steady shear viscosity and elastic modulus at higher concentrations when a homogeneous entangled network is reached. We attribute this behavior to the semirigid character of the hyaluronan chain and to the predominance of entanglements over the cross-link points present in hylan in the semidilute domain. Due to the higher apparent molecular weights that are possible with hylan structures but not with the hyaluronans currently available, a wider range of applications can be achieved with hylans when viscoelasticity is required, particularly for the viscosupplementation of synovial fluid damaged by osteoarthritis.