Slow lowering of pH induces gel formation of myosin

It has been found that solutions of myosin (10 mg/ml) form gels at 5°C if the pH is decreased slowly, by dialysis, to a value in the region of 2.5 to 5.5. Gel strength displays strong dependence on final pH, having a maximum at about pH 4.5. Salt (KCl) concentration was found to affect gel strength positively and linearly. Differential scanning calorimetry revealed that the myosin of pH-induced gels absorbed no thermal energy when heated, implicating acid-induced denaturation as the basis of gel formation. By comparison with heat-induced gelation of myosin and from the fact that low pH is conducive to filament formation, it is suggested that filaments may also be involved in the gelation process.     

Dynamic rheological measurements on heat-induced myosin gels: Effect of ionic strength,protein concentration and addition of adenosine triphosphate or pyrophosphate

Myosin solutions and suspensions have been monitored during heating at pH 6.0 by using dynamic rheological measurements. The storage modulus (G′), the loss modulus (G) and the phase angle (δ) all showed a marked dependence on ionic strength in the temperature range 25–75°C. The filamentous gels (ionic strength <0.34) displayed a temporary reduction in G′ at temperatures between 50 and 60°C, presumably due to denaturation in parts of the rod portion of the myosin molecule. In the same temperature region the concentration dependence of G′ changed by a power of 2. The loss modulus also showed a marked concentration dependence, while the phase angle varied with concentration primarily at low (<50°C) temperatures. For the final gels, heated to 75°C, only G′ indicated marked differences due to different protein concentrations and ionic strengths; all gels were almost completely elastic (δ?1°). Adenosine triphosphate was shown to have a pronounced temporary effect on the filamentous gel formed at low temperatures, i.e. on the gel with the highest concentration dependence, while pyrophosphate had no such effect. However, both adenosine triphosphate (or rather its hydrolysis product: adenosine diphosphate) and pyrophosphate appeared to have a small, lasting effect on the heat-gelling ability of myosin: the former a detrimental effect, the latter an improvement.     

Polycyclic aromatic hydrocarbons in grilled meat products—A review

Current efforts to detect and quantify carcinogenic polycyclic aromatic hydrocarbons (PAH) in the environment include analyses of foods. Grilled foods have been under scrutiny for almost 20 years. In this review reports concerning PAH contamination of grilled meat products are discussed. It is evident that the level of contamination varies considerably, primarily due to the extent of fat pyrolysis which has taken place. If proper precautions against fat pyrolysis are taken, and out-of-the-ordinary fuels such as crumpled paper or cones are not used, the PAH contamination is reduced substantially. Furthermore, if the relatively low consumption of grilled meat products is taken into consideration public concern over possible health risks due to grilling appears unwarranted.     

Formation of complexes between lecithin and apovitellenin I,an avian egg-yolk apoprotein

In a study of lipid-protein interactions in egg yolk, it was found that L-α-dipalmitoyl lecithin gave two distinct noncovalent complexes (A and B) with apovitellenin I, an apoprotein in the major yolk lipoprotein. Interaction took place under widely varied conditions, and yolk lecithin gave similar complexes. Complex A, which was formed within minutes, consisted of round particles of about 9 nm diameter. Complex B, which was formed more slowly, consisted of larger, particles. Possibly resembling curved discs, with diameter of 30–40 nm. The preparation and some properties of these complexes are described. It is suggested that they may be suitable for an extensive study of phospholipid-protein interactions in yolk.     

Effects of electrical stimulation and ageing of beef on the gelation properties and protein extractability of isolated myofibrils

The gelation properties of bovine myofibrils, as evaluated by dynamic rheological measurements, were shown to be very sensitive to the variables investigated: stimulation and/or ageing of the meat used, presence of 5 mM pyrophosphate and 5 mM MgCl₂ (PP) and concentration of NaCl (0·3 or 0·M). Statistical evaluation of final gel storage moduli (determined at 70°C) revealed ageing to have a consistent detrimental effect. Fresh, stimulated processing of meat), gave gels of about 40% lower elasticity (storage modulus) than did non-stimulated myofibrils; when PP was included in the gel-forming mixture no effect from electrical stimulation was seen. In spite of the negative effects observed for gel elasticity, the myofibrils in question displayed enhanced protein extractability prior to heating. Electrophoretic results suggest myosin degradation to be partly responsible.     

Myosin denaturation in pale, soft, and exudative (PSE) porcine muscle tissue as studied by differential scanning calorimetry

Myofibrillar tissue from pale, soft, and exudative (PSE) pork was compared to tissue from normal pork by differential scanning calorimetry at pH 5.4. Thermograms of myofibrillar tissue from normal pork were characterised by three major peaks with temperature maxima at 58 and 66°C, associated with myosin denaturation, and at 78°C, associated with actin denaturation. In thermograms of PSE pork, the peak at 58°C was markedly reduced, and appeared as a shoulder. When the thermograms were divided into segments corresponding to the three major peaks, the area of the low temperature myosin segment was shown to be reduced by about 50% in PSE pork, as compared to normal pork. This indicates approximately 50% denaturation of the least thermostable parts of the myosin molecule. The more thermostable parts of the myosin molecule were largely unaffected, as was actin.     

Myosins from red and white bovine muscles: Differences measured by turbidimetric,calorimetric and rheological techniques

The aim of this study was to elucidate the functional performance of the most abundant protein component in meat, ie myosin, which is recognised as important for binding in meat products. As several genetic variants of skeletal myosin exist, myosins from two bovine muscles of different fibre type composition, M masseter and M cutaneus trunci were compared with respect to filament forming properties and denaturation characteristics. The principal methods used were turbidimetric measurements, which were used to monitor filament formation, calorimetry and rheology. The myosin systems were examined at two different salt levels (0.2 and 0.6 M NaCl) and at pH 5.5–7.0. The method of preparing myosin suspensions/solutions was also examined. Differences in the filament-forming process for the two myosins were detected. Measurements of turbidity revealed that at conditions of low pH and low ionic strength white myosin had a higher ultimate turbidity compared with red myosin. Early in the transition from low to high turbidity, red myosin had a higher turbidity than white myosin corresponding to reduced solubility. The turbidity increased with time of storing the myosin suspensions/solutions. This change was attributed to formation of filaments and further association of filaments. White myosin had a smaller apparent enthalpy of denaturation than red myosin. The calorimetric measurements recorded in 0.2 M NaCl suggested that the head and the rod of white myosin were less stable than the corresponding parts of red myosin. However, exceptions to this rule were found at pH 6.0. In 0.6 M NaCl the identification of the transitions for red myosin was more difficult. The method of preparing myosin suspensions affected calorimetric and rheological measurements. In 0.6 M NaCl and pH 6.0 calorimetric thermograms of both myosins were affected by the preparation method. At pH 5.5 this change was interpreted as caused by denaturation promoted by the dilution/rapid titration technique compared with dialysing the systems to pH 5.5 from pH 7. Differences in the filaments formed might, however, also contribute to the variations seen in the calorimetric ther-mograms. The gelling properties of white myosin were most sensitive to the preparation method used. Systems prepared by dialysis gave stronger heat-induced gels than those prepared by ‘dilution’. White myosin always produced stronger gels than red myosin independent of the preparation technique. The rheological properties (at 80°C) of red myosin were less affected by the preparation method than were those of white myosin. At lower temperatures, however, there was more variation in the shapes of the rheological thermograms (? versus temperature) for red myosin than in the corresponding thermograms of white myosin.     

受管制电网公司在鼓励基础上的风险管理

引　言电网作为天然的垄断事业而且在多数国家是按放宽管制的电力市场方式进行管制的。直到 1997年 ,挪威都是按照投资收益率准则 (ＲＯＲ)来管制其配电公司。经验表明 ,有关投资、运营、检修方面的风险很低 ,成本回收是得到保证的 ,但这意味着 ,用户不得不承担超额的投资和高额的运营成本。此外 ,投资收益率是根据其帐面价值计算的 ,因此 ,电网公司被给以投资额外输变电容量的鼓励。投资收益率管理在挪威实行了很长一段时间后 ,1997年引进了一种综合了基于鼓励的管制与基于业绩的制定费率制度。这种模式融合了有基准的收入封顶的管制和收益…     

Dynamic rheological measurements on heat-induced myosin gels: An evaluation of the method's suitability for the filamentous gels

Formation of bovine myosin gels (10 mg ml^?1) by heat treatment at pH 6 and an ionic strength of 0.24 M has been monitored by using the Bohlin Rheometer System in the oscillatory mode. Rheological thermograms were determined with a general repeatability of about 2% for a given suspension. A pronounced maximum and an accompanying minimum in storage modulus (G′) were found at about 50 and 55°C, respectively. The thermograms for the loss modulus (G″) and the phase angle (δ) displayed complex behaviour as well, suggesting a multitransition process. Presumably, denaturational events in parts of the molecule are responsible for the complex rheology observed. This complexity is not related to trivial wall slippage as data obtained from cells with different gap sizes were highly reproducible and consistent with other measurements. A decrease in heating rate from 2.5 to 0.1°C min^?1 had a large effect on G′; it increased from 905 to 1600 N m^?2 for gels at 75°C. The phase angle was also affected by the heating rate, especially at about 55°C. The effect of increasing the strain from 0.003 to about 0.1 was significant in two temperature regions; G′ at temperatures higher than 65°C and δ at temperatures lower than 54°C increased with increasing strain.