Thawing of lamb loin chops in air and CO(2). Effect on colour and drip

Colour retention and drip loss was assessed during retail display for chilled lamb chops displayed fresh or stored in CO(2) for 7 weeks before display, and for chops frozen for various times and thawed in air or CO(2). A sensory panel found fresh lamb chops to have an acceptable display life of 1 day, while chops which had been frozen for 1 day and then thawed lasted 2 days. Holding chops for 7 weeks in a CO(2) atmosphere at - 1·5°C improved display life to 3 days, but frozen chops held for 7 weeks before thawing had deteriorated in colour, and only one group was acceptable on the initial day of display. Initially there were no differences in Hunter L values (brightness) due to treatment, but chilled chops or those frozen for 1 day showed a greater increase in L values by the second day than those frozen for 7 weeks, after which there was no change in brightness. Hunter a values (redness) were higher in chilled chops and those thawed after 1 day's frozen storage than those frozen for 7 weeks before thawing. Hunter b values (yellowness) were greater at all times in chilled chops held for 7 weeks and varied amongst the other treatments. The measured per cent drip from chops frozen for only 1 day was greater on thawing than drip from chops frozen for 7 weeks before thawing. Drip during display, assessed by a sensory panel, increased more in those chops stored either chilled or frozen for 7 weeks before display.     

Effect of tray liners on the drip loss of lamb chops during retail display

The amount of drip lost by lamb chops during display was affected by the type of tray liner used. In one study involving chilled and frozen/thawed meat, the use of an absorbent paper liner increased the drip loss and influenced whether or not the quantity of drip was affected by freezing/thawing. In another study, thawed chops held for 24 h on plastic coated trays without liner or on a plastic coated liner had less than 2% drip loss, whereas adjacent chops from the same loin processed and held in the same way but displayed on liners of absorbent paper or paper pouches of diatomaceous earth lost 4·3% and 5·6% drip, respectively. This effect of the material in contact with the meat should be considered when reporting drip loss data and when comparing results with those of other researchers.     

Supercritical fluid extraction and characterization of lipids from algae Scenedesmus obliquus

Supercritical carbon dioxide (SC-CO2) extractions (with and without ethanol as an entrainer) were carried out to remove lipids and pigments from protein concentrate of green algae (Scenedesmus obliquus) cultivated under controlled conditions. The content and fatty acid composition of algal lipids using column, thin-layer (TLC) and gas-liquid chromatography (GLC) were determined. Absorption spectra of extracted fractions showed the predominance of chlorophyll A (lambda max at 410 nm). Single step supercritical carbon dioxide (SC-CO2) extraction resulted mostly in removal of neutral lipids and a part of glycolipids, but phospholipids were not extracted. Addition of ethanol to SC-CO2 increased the amount of glycolipids and phospholipids in the extract. TLC pattern of algal lipids showed that the main part of neutral lipids consisted of diglycerides, triglycerides, hydrocarbons, free sterols, and sterol esters. The glycolipids were mostly monogalactosyl diglyceride, digalactosyl diglyceride, esterified sterol glycoside, and sterol glycoside. In phospholipids, phosphatidyl choline, phosphatidyl glycerol, and phosphatidyl ethanolamine were the main compounds. Fatty acid composition patterns indicated the main fatty acids to be 16:0, 16:1, 16:2, 16:3, 16:4, 18:1, 18:2, and 18:3(a). Relatively high recovery of polyunsaturated fatty acids and essential fatty acids in supercritical fluid extracted algal lipids and proteins isolates were observed.     

NanoProbeArrays for the analysis of ultra-low-volume protein samples using piezoelectric liquid dispensing technology

Antibody microarrays are gaining popularity as a high-throughput technology to investigate the proteome. However, protein extracts from most body fluid or biopsy samples are available in very small volumes and are often unsuitable for large-scale antibody microarray studies. To demonstrate the potential for protein analysis with as little as a few nanoliters of sample, we have developed a new technology called NanoProbeArrays based on piezoelectric liquid dispensing for non-contact printing and probing of antibody arrays. Instead of flooding the protein sample on the antibody microarray surface, as in conventional microarray screening, a piezoelectric inkjet printer is used to dispense nanoliters of fluorescently labeled proteins over the antibody spots on the array. The ability of NanoProbeArrays to precisely identify and reliably distinguish between test proteins from different sources, without any loss of sensitivity and specificity as compared with conventional antibody microarrays, is illustrated here. The utility of NanoProbeArrays for biomarker identification in a complex biological sample was tested by detecting the cytokine interleukin-4 in serum. The significant reduction in volume of sample during NanoProbeArray analysis, as compared with conventional antibody microarrays, offers new opportunities for basic and applied proteomic research.     

新一代微机变电站保护的智能化措施

提出变电站微机保护实现智能化的具体方式。从保护装置投入运行前后的调试、生产、维护各方面，就人机界面、信息通信等方面分析具体智能化措施。     

Aequorin-based functional assays for G-protein-coupled receptors,ion channels,and tyrosine kinase receptors

Aequorin is a photoprotein originating from jellyfish, whose luminescent activity is dependent on the concentration of calcium ions. Due to the high sensitivity and low background linked to luminescent assays, as well as to its absence of toxicity and its large linear dynamic range, aequorin has been used as an intracellular calcium indicator since its discovery in the early 1960s. The first applications of aequorin involved its microinjection in cells. The cloning of its gene in 1985 opened the way to the stable expression of aequorin in cell lines or even entire organisms. Here we present the validation of aequorin as a functional assay for the screening of G-protein-coupled receptors, ion channels, and tyrosine kinase receptors, as well as for their pharmacological characterization in agonist and antagonist detection assays. We optimized our cell suspension-based assay and determined that the most sensitive assay was performed at room temperature, with mitochondrially expressed aequorin and using coelenterazine derivative h for reconstitution of aequorin. The robustness of the assay and the current availability of luminometers with integrated injectors allow aequorin to fit perfectly with high throughput functional assays requirements.