Effects of L- or D-lactate-enhancement on the internal cooked colour development and biochemical characteristics of beef steaks in high-oxygen modified atmosphere

The effects of L- or D-lactate on internal cooked colour development of steaks packaged in high-oxygen (80% O₂/20% CO₂) modified atmosphere packaging (MAP) was investigated. Ten USDA Select beef strip loins were divided individually into 4 equal-width sections, and one of four treatments (control, 0.3% sodium tripolyphosphate, 2.5% L-lactate + 0.3% sodium tripolyphosphate, and 2.5% D-lactate + 0.3% sodium tripolyphosphate) was assigned randomly to the loin sections. Loin sections were injected to approximately 10% of their raw weight. Steaks packaged in high-oxygen MAP were stored in the dark at 1 °C for 10 days. Instrumental internal colour of raw and cooked steaks (70 °C), total reducing activity (TRA), NADH concentration, and percent myoglobin denaturation (PMD) were measured. Cooked steaks enhanced with 2.5% L-lactate/phosphate maintained higher a*/b* ratios, lower hue values, higher TRA and NADH concentration, and lower PMD than the control and D-lactate-injected steaks, whereas enhancement with 2.5% D-lactate did not affect cooked colour, TRA, NADH, or PMD. Thus, inclusion of an L-lactate/alkaline phosphate blend increased the reducing activity of muscle tissues by replenishing NADH and subsequently decreased the thermal denaturation of myoglobin by maintaining the reduced state of myoglobin in the high-oxygen package.     

NMR relaxometry and differential scanning calorimetry during meat cooking

By combining simultaneous nuclear magnetic resonance (NMR) T₂ relaxometry and differential scanning calorimetry (DSC) on pork samples heated to nine temperature levels between 25 and 75 °C, the present study investigates the relationship between thermal denaturation of meat proteins and heat-induced changes in water characteristics. Principal component analysis (PCA) on the distributed ¹H NMR T₂ relaxation data revealed that the major changes in water characteristics during heating occur between 40 and 50 °C. This is probably initiated by denaturation of myosin heads, which however, could not be detected in the DSC thermograms obtained directly on the meat. In contrast, the DSC thermograms revealed endothermic transitions at 54, 65 and 77 °C, probably reflecting the denaturation of myosin (rods and light chain), sarcoplasmic proteins together with collagen and actin, respectively. Simultaneous modelling of DSC and NMR data by partial least squares regression (PLSR) revealed a correlation between denaturation of myosin rods and light chains at 53–58 °C and heat-induced changes in myofibrillar water (T₂ relaxation time 10–60 ms) as well as between actin denaturation at 80–82 °C and expulsion of water from the meat. Accordingly, the present study demonstrates a direct relationship between thermal denaturation of specific proteins/protein structures and heat-induced changes in water mobility during heating of pork.     

紫外分光光度法鉴别复原奶和保鲜奶

对保鲜奶和复原奶中未变性乳清蛋白质量浓度的差别进行研究，初步探索了以紫外分光光度法对二者进行快速鉴别的方法。通过对未变性乳清蛋白的吸光度的研究确定了它的最大吸收波长为292nm，可在此波长下测出它的吸光度值并由标准曲线的线性回归方程算得其质量浓度。结果表明，复原奶中的未变性乳清蛋白质量浓度与保鲜奶中未变性乳清蛋白质量浓度差异较大。测量结果与凯氏定氯法的测量结果进行比较，这种方法与凯氏定氯法无显著差异，但此法较为简易，实用性较强。     

船用碳锰钢钙处理研究

分析硅钙线和纯钙线对控制钢中夹杂物变性的影响效果。通过合理控制钢中钙、铝、硫含量,使夹杂物充分变性和去除,可以稳定提高超声检测合格率。     

低值鱼蛋白的热变性与酶解特性关系研究

本文选用低值鱼为对象，研究它们在不同的热处理条件下蛋白变性程度、-SH含量变化及它们对酶解特性的影响。DSC扫描曲线显示：热处理温度升高、时间延长，变性程度增大，80℃，10min蛋白变性程度已达98．31％。酶解结果表明除60℃外，80℃和100℃均不利于酶解。热变性后蛋白中-SH含量与TCA可溶性氮成较好线性关系。     

Biodegradable plastics from animal protein coproducts: Feathermeal

This work describes the properties of plastics made from partially denatured proteins produced by the animal coproduct (rendering) industry and these plastics' fabrication. Specifically, plastic samples from partially denatured feathermeal protein were successfully produced by a compression‐molding process. The modulus (stiffness) of the material obtained was found to be comparable with that of commercial synthetic materials, such as polystyrene, but was found to have lower toughness characteristics, which is a common phenomenon among plastics produced from animal and plant proteins. A reversible stress–strain property was observed over the yield region. Plastic‐forming conditions for undenatured animal proteins, such as albumen and whey proteins, were also formulated for fabricating plastics out of these proteins' blends with feathermeal proteins. The resultant plastic samples that were developed of biomacromolecular blends, such as feathermeal/whey and feathermeal/albumen, demonstrated improved mechanical properties, specifically tensile strength, when compared with neat plastics from feathermeal proteins. The values for the stiffness of the feathermeal/whey blends deviated from simple mixing rule and showed a synergistic effect. © 2008 Wiley Periodicals, Inc. J Appl Polym Sci, 2008     

Kinetic and Thermodynamic Parameters for Heat Denaturation of Cry1A(b) Protein from Transgenic Maize (Zea mays)

ABSTRACT:  The effect of heat treatment on the denaturation of Cry1A(b) protein expressed in transgenic maize was studied over a temperature range of 69 to 77 °C. Denaturation of Cry1A(b) protein was measured by the loss of reactivity with its specific antibodies using a sandwich ELISA. The process of denaturation was studied by analyzing the values of inmunoreactive protein after each heat treatment by kinetic analysis. Denaturation of Cry1A(b) protein was best described assuming a reaction order of 1.5. D -values calculated were 4338, 2350, 1272, 734, and 601 s at 69, 71, 73, 75, and 77 °C, respectively. Z -value was estimated to be 9.0 °C and the activation energy value was 266.15 kJ/mol. Thermodynamic parameters for the process of denaturation of Cry1A(b) protein were also calculated. The high values of the enthalpy of activation and the positive values of the entropy of activation obtained for Cry1A(b) protein are typical of a reaction in which the denaturation of the protein is the rate-determining process that predominates over an aggregation process during heating.     

优化蛋清粉蛋白热变性条件的研究

为了降低蛋清粉蛋白高F值寡肽的生产成本以实现工业化大规模生产,本实验利用了对比分析和L9(34)正交试验设计方法,考察热变性时间、热变性温度和加酶量三个因素对蛋清粉蛋白水解度的影响,优化出蛋清粉蛋白热变性条件的最佳参数为:当底物浓度为5%,热处理温度90℃,热处理时间10min,碱性蛋白酶加酶量5%,酶解5h后蛋清粉蛋白水解度为26.68%。