Determination of anti-oxidative histidine dipeptides in poultry by microchip capillary electrophoresis with contactless conductivity detection.

A home-made microchip electrophoresis (MCE) device was used to quantitate two biologically important histidine dipeptides, carnosine and anserine, using capacitively coupled contactless conductivity detection (C4D), at pH 2.7. The C4D detector exhibited a linear response to both carnosine and anserine in the range of 0-200µM for the individual dipeptides and in the range of 0-100µM for each dipeptide when both were present as a mixture. The limit of detections (LOD) for the dipeptides in the mixture were 0.10µM for carnosine and 0.16µM for anserine. Standard addition was used to detemine the accuracy of the method. For carnosine and anserine the recoveries were in the range of 96.7±4.9-106.0±7.5% and 95.3±4.5-105.0±5.1% in thigh muscle and 97.5±5.1-105.0±7.5% and 95.3±5.4-97.3±5.6% in breast muscle, respectively.

Solubilisation of myosin in a solution of low ionic strength L-histidine: Significance of the imidazole ring.

Myosin, a major muscle protein, can be solubilised in a low ionic strength solution containing L-histidine (His). To elucidate which chemical constituents in His are responsible for this solubilisation, we investigated the effects of 5mM His, imidazole (Imi), L-α-alanine (Ala), 1-methyl-L-histidine (M-his) and L-carnosine (Car) on particle properties of myosin suspensions and conformational characteristics of soluble myosin at low ionic strength (1 mM KCl, pH 7.5). His, Imi and Car, each containing an imidazole ring, were able to induce a myosin suspension, which had small particle size species and high absolute zeta potential, thus increasing the solubility of myosin. His, Imi and Car affected the tertiary structure and decreased the α-helix content of soluble myosin. Therefore, the imidazole ring of His appeared to be the significant chemical constituent in solubilising myosin at low ionic strength solution, presumably by affecting its secondary structure.

A hydrophilic interaction liquid chromatography-mass spectrometry (HILIC-MS) based metabolomics study on colour stability of ovine meat.

Meat colour is one of the cues available to the consumer to gauge overall meat quality and wholesomeness. Colour stability of meat is determined by several factors both inherent to the animal and post-slaughter conditions, including ageing, storage/packaging and display times. A hydrophilic interaction liquid chromatography-mass spectrometry (HILIC-MS) based metabolomics study was undertaken to identify and compare polar metabolites between ovine meat samples that were exposed to different durations of ageing, storage conditions, and display times. Primary metabolites comprising amino acids, sugars, nucleotides, nucleosides, organic acids and their breakdown products were mainly identified as discriminating factors. For the first time, boron complexes of sugar and malic acid were also tentatively identified. As expected, most compounds identified were related to myoglobin chemistry, and compounds with antioxidant properties were found in higher levels in colour stable samples. Supplementary studies identifying semi-polar, non-polar and volatile compounds will provide a holistic understanding of the chemical basis of colour stability in ovine meat.