Application of proteomics to understand the molecular mechanisms behind meat quality.

The proteome is expressed from the genome, influenced by environmental and processing conditions, and can be seen as the molecular link between the genome and the functional quality characteristics of the meat. In contrast to traditional biochemical methods where one protein is studied at a time, several hundred proteins can be studied simultaneously. Proteomics is a promising and powerful tool in meat science and this is reflected by the increasing number of studies emerging in the literature using proteomics as the key tool to unleash the molecular mechanisms behind different genetic backgrounds or processing techniques of meat. Thus understanding the variations and different components of the proteome with regard to a certain meat quality or process parameter will lead to knowledge that can be used in optimising the conversion of muscles to meat. At present, there has been focus on development of techniques and mapping of proteomes according to genotypes and muscle types. In the future, focus should be more towards understanding and finding markers for meat quality traits. This review will focus on the methods used in the published proteome analyses of meat, with emphasis on the challenges related to statistical analysis of proteome data, and on the different topics of meat science that are investigated.

Variation in the response to manipulation of post-mortem glycolysis in beef muscles by low-voltage electrical stimulation and conditioning temperature.

The aim of this study was to investigate how manipulation of glycolytic rate by post-mortem processing conditions influences quality of aged beef of two bovine muscles of different physiological character, longissimus dorsi (LD) and adductor (AD). Post-mortem glycolysis was manipulated by low-voltage electrical stimulation (LV-ES) of half carcasses and by chilling rate of the muscles. Multivariate statistical analysis was used to visualise the data, while ANOVA was used to identify significant effects and interactions. As expected there was a significant effect of LV-ES on the pH decline in the first hours post-mortem in both muscles. Moreover, significant effects of LV-ES on WB shear force measured 2 and 8 days after slaughter were observed for LD at both chilling temperatures, while for AD no effect on WB shear force was observed. Furthermore, the results revealed a large individual variation in the response of LV-ES on both pH decline and WB shear force, and this variation did not always correlate for the two responses. Some animals showed no response of LV-ES on pH decline, but still had an improved WB shear force, and vice versa. The results from this study indicate that there probably are other mechanisms than accelerated pH decline and prevention of cold-shortening, by which LV-ES can affect meat tenderness.

Accelerated recovery of Atlantic salmon (Salmo salar) from effects of crowding by swimming.

The effects of post-crowding swimming velocity (0, 0.35, and 0.70 m/s) and recovery time (1.5, 6, and 12 h) on physiological recovery and processing quality parameters of adult Atlantic salmon (Salmo salar) were determined. Atlantic salmon crowded to a density similar to that of a commercial slaughter process (>200 kg/m(3), 40 min) were transferred to a swimming chamber for recovery treatment. Osmolality and concentrations of cortisol, glucose and lactate in blood plasma were used as physiological stress indicators, whereas image analyses of extent and duration of rigor contraction, and fillet gaping were used as measures of processing quality. Crowded salmon had a 5.8-fold higher plasma cortisol concentration than control salmon (P<0.05). The elevated plasma cortisol concentration was reduced by increasing the swimming velocity, and had returned to control levels after 6 h recovery at high water velocity. Similar effects of swimming velocity were observed for plasma osmolality and lactate concentration. A lower plasma glucose concentration was present in crowded than in control fish (P<0.05), although a typical post-stress elevation in plasma glucose was observed after the recovery treatments. Lower muscle pH was found in crowded compared with control salmon (P<0.05), but muscle pH returned to control levels after 6 h recovery at intermediate and high swimming velocities and after 12 h in the low velocity group. Crowding caused an early onset of rigor mortis contraction. However, subjecting crowded salmon to active swimming for 6 h before slaughter delayed the onset of rigor mortis contraction from 2.5 to 7.5 h post mortem. The extent of rigor mortis contraction was also affected by crowding and post-stress swimming activity (P<0.05), and the largest degree of contraction was found in crowded salmon. In conclusion, active swimming accelerated the return of plasma cortisol, hydromineral balance, and the energy metabolism of adult Atlantic salmon to pre-stress levels. Moreover, an active swimming period delayed the onset of rigor mortis contraction, which has a positive technological implication for the salmon processing industry.

Meat tenderness and muscle growth: is there any relationship?

Our objectives for this manuscript are to review the mechanisms of muscle growth, the biological basis of meat tenderness, and the relationship between these two processes. Muscle growth is determined by hyperplasia and hypertrophy. Muscle cell size is determined by the balance between the amount of muscle protein synthesized and the amount of muscle protein degraded. Current evidence suggests that the calpain proteolytic system is a major regulator of muscle protein degradation. Sarcomere length, connective tissue content, and proteolysis of myofibrils and associated proteins account for most, if not all, of the explainable variation in tenderness of meat after postmortem storage. The relative contribution of each of the above components is muscle dependent. The calpain proteolytic system is a key regulator of postmortem proteolysis. While changes in muscle protein degradation affect meat tenderization/tenderness, changes in muscle protein synthesis are not expected to affect meat tenderization/tenderness.