Effects of blade tenderization,aging method and aging time on meat quality characteristics of Longissimus lumborum steaks from cull Holstein cows

The effects of blade tenderization (BT), two aging methods (dry (D) and wet (W)), and aging time (2 and 23 d) on tenderness, color, and sensory properties of Longissimus lumborum muscles from 12 cull Holstein cows were evaluated. Dry-aged loins had higher combined trim and aging losses than control (C) for both D- and W-aging, mostly because of excess trim losses. BT steaks had WBSF of 33.13 N while C steaks had WBSF of 41.46 N (P = 0.09). Aging decreased WBSF. Blade tenderized steaks had higher cook loss than C steaks. Aging, W-aging, and BT × W-aging improved myofibrillar (sensory) tenderness scores. Aging and/or BT improves sensory panel tenderness cull cow Longissimus lumborum steaks. Aging and blade tenderization combined can increase tenderness and value of Longissimus steaks from cull Holstein cows.     

Biomarkers of meat tenderness: Present knowledge and perspectives in regards to our current understanding of the mechanisms involved

Biomarkers of the meat quality are of prime importance for meat industry, which has to satisfy consumers' expectations and, for them, meat tenderness is and will remain the primary and most important quality attribute. The tenderization of meat starts immediately after animal death with the onset of apoptosis followed by a cooperative action of endogenous proteolytic systems. Before consideration of the biomarkers identified so far, we present here some new features on the apoptotic process. Among them, the most important is the recent discovery of a complex family of serpins capable to inhibit, in a pseudo-irreversible manner, caspases, the major enzymes responsible of cell dismantling during apoptosis. The biomarkers so far identified have been then sorted and grouped according to their common biological functions. All of them refer to a series of biological pathways including glycolytic and oxidative energy production, cell detoxification, protease inhibition and production of Heat Shock Proteins. Some unusual biomarkers are also presented: annexins, galectins and peroxiredoxins. On this basis, a detailed analysis of these metabolic pathways allowed us to identify some domains of interest for future investigations. It was thus emphasized that mitochondria, an important organelle in the production of energy from carbohydrates, lipids and proteins are a central element in the initiation and development of apoptosis. It was therefore stressed forward that, in fact, very little is known about the postmortem fate of these organelles and their multiple associated activities. Other topics discussed here would provide avenues for the future in the context of identifying reliable predictors of the ultimate meat tenderness.     

A comparison between the effects of day and night cropping on gemsbok (Oryx gazella) meat quality

This study compares the effects of day- and night cropping on the quality of gemsbok meat. Day-cropped animals had higher behavioural scores and cortisol levels (behavioural score: 3.5 ± 0.423; cortisol: 136.88 ± 2.731 nmol/L) than night-cropped animals (behavioural score: 2.1 ± 0.378; cortisol: 64.1 ± 1.633 nmol/L) while night-cropped animals had a higher mean pH_u (5.54 ± 0.013) than day-cropped animals (5.49 ± 0.014). The exponential decay model, y = a + b^−ct, fitted to the pH data indicated a difference in constant a only (day = 5.45 ± 0.006; night = 5.51 ± 0.006). Night-cropped animals produced meat that was darker in colour. The results indicate that day cropping may have elicited more ante-mortem stress although this did not necessarily affect the meat quality adversely, however due to the limitation of sample size, the data may be skewed by outliers and should thus be interpreted with caution.     

Shelf life extension of beef retail cuts subjected to an advanced vacuum skin packaging system

Vacuum skin packaging (VSP) is a new and promising technology that includes the instantaneous heating of the upper packaging film immediately before its descent over the meat surface. In the present paper we evaluated this technology for the packaging of a wide variety of beef retail cuts and compared this with traditional vacuum packaging (TVP) performed in parallel. Shelf-life and quality evolution was estimated by analysing three spoilage bacterial groups, an ubiquitous psychrotrophic food pathogen, and three biochemical and physico-chemical attributes throughout 40 days of storage at 4 °C. Statistically-significant lower microbial counts were obtained for all microbial parameters and meat types. The VSP lot exhibited lower pH. This, however, involved a lower water holding capacity and a higher degree of firmness, the latter indicating a limited tenderisation process in the VSP batch. Extended aging times in the carcasses were studied to improving the tenderness of VSP samples. The extension of the aging process prior to VSP may be useful for improving the tenderness of certain meat types and to improve the sensory quality of meat cuts processed under this system.     

Evidence against the non-enzymatic calcium theory of tenderization

The objective of the present study was to determine whether variation in the tenderization of lamb longissimus could be attributed to variations in the rise in free calcium postmortem and sarcomere lengthening post rigor. The longissimus muscle of 10 crossbred lambs (Romney×Coopworth) was sampled at 1 and 7 days postmortem for determination of MIRINZ shear force, myofibrillar fragmentation index (MFI), sarcomere length, free calcium, and proteolysis of troponin-T. Despite considerable variation in tenderness and tenderization of the muscles, sarcomere lengthening was not observed. The concentration of free calcium at 7 days postmortem correlated significantly with the MFI (r=0.640; P<0.05) and tended to correlate with the shear force (r=−0.596; P<0.1) and degradation of troponin-T (r=0.625; P<0.1). Degradation of troponin-T was significantly correlated with tenderization (r=0.664; P<0.05). Troponin-T is a calpain substrate, but reportedly is not degraded through a direct effect from calcium. The present results, therefore, suggest that the variation in free calcium in postmortem muscle affects tenderization through an effect on the calpain system and not through a direct effect of calcium on myofibrillar proteins. Consequently, the results of this study do not support the (calcium) theory that calcium directly affects tenderization.     

Biochemistry of postmortem muscle — Lessons on mechanisms of meat tenderization

It is certain that meat tenderness is a highly valued consumer trait and thus definition of the multiple processes that influence meat tenderness will provide clues toward improving meat quality and value. The natural process by which meat becomes tender is complex. Tenderness development is dependent on the architecture and the integrity of the skeletal muscle cell and on events that modify those proteins and their interaction. Specifically protein degradation and protein oxidation have been identified as processes that modify proteins as well as the tenderness of meat. The intracellular environment is a major factor that controls these events. Ultimately, the interplay between these events determines the rate and extent of tenderization. Given the intricacy of the structure of the muscle cell, coupled with the complexity of the regulation of protein modification and the ever-changing intracellular environment it is not surprising that this area of research is a very dynamic field. Just as the overall integrity and function of muscle cells does not depend on a single protein, but rather on the coordinated interaction of several proteins, the structural weakening of muscle cells during postmortem aging also must not depend on the degradation of a single myofibrillar or other cytoskeletal protein. The proteins mentioned in this review are located in different regions of the muscle cell, and most have been implicated in some manner as being important in maintaining the structure and function of the muscle cell. Oxidation of myosin heavy chain, a predominant protein in the myofibril, is known to promote aggregation and toughening of meat. Degradation of proteins such as desmin, filamin, dystrophin, and talin (all located at the periphery of the Z-line) may disrupt the lateral register and integrity of the myofibril themselves as well as the attachments of the peripheral layer of myofibril to the sarcolemma. Degradation of the proteins within the myofibril that are associated with the thick and thin filaments may allow lateral movement or breaks to occur within the sarcomeres of postmortem aged samples. Titin, nebulin, and troponin-T, by their ability to directly interact with, or modulate the interaction between, major proteins of the thick and thin filaments and (or) the Z-line, play key roles in muscle cell integrity. Disruption of these proteins, especially titin and nebulin, could initiate further physicochemical and structural changes that result in myofibril fragmentation and loss of muscle cell integrity, and ultimately in tenderization of the muscle. In order to make real progress in this area, the scientific community must have a global appreciation of how both the structural proteins and the key proteases are influenced by the vast changes that occur during the conversion of muscle to meat.     

Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes--a review

This paper reviews current knowledge on the distribution and mobility of water in muscle (myowater) ante- and post mortem and factors affecting these in relation to fresh meat quality parameters; water-holding capacity (WHC), tenderness and juiciness. NMR transverse relaxometry (T(2)) using bench-top Low-Field Nuclear Magnetic Resonance (LF-NMR) has characterised myowater distribution and mobility as well as structural features in meat which directly affect WHC. The current literature demonstrates that WHC is correlated to the water located outside the myofibrillar network (extra-myofibrillar). This review identifies the critical stages which affect the translocation of water into the extra-myofibrillar space and thus the potential for decreased WHC during proteolysis (the conversion of muscle to meat). This review discusses how the intrinsic properties of the water held within the meat could contribute to juiciness and tenderness. Tenderness has been shown to correlate to T(2), however breed and species differences made it difficult to draw firm conclusions. Further understanding of the inherent water properties of fresh meat and the factors affecting water distribution and mobility using NMR technologies will increase the understanding of WHC and tenderisation of fresh meat.     

Effect of cooking temperature and time on the physico-chemical, histological and sensory properties of female carabeef (buffalo) meat

The effect of cooking temperature (80-100°C) and time (30-60min) on collagen solubility of Semimembranosus muscle in carabeef were investigated. The pH, cooking loss, shear force value, collagen content, collagen solubility, sensory evaluation and histological observations of water bath cooked and pressure cooked Semimembranosus meat samples were measured. Increase in pH, cooking loss, collagen solubility and tenderness scores with decrease in shear force value and collagen content was observed with increases in cooking temperature and time. However, no statistical difference was observed for shear force values, collagen solubility values and tenderness scores in pressure cooked meat and meat cooked in a water bath at 100°C for 45min, inferring that cooking of buffalo meat at 100°C for 45min improved collagen solubility and tenderness to the same extent as that due to pressure cooking.     

Effect of age and cut on tenderness of South African beef

The tenderness characteristics of 15 primal cuts of beef of three different age groups were assessed, and the most reliable cut to predict carcass tenderness was determined. Fifteen wholesale cuts from each age group, representing the full variation in fatness, were aged, cooked and underwent sensory evaluation, shear force resistance and proximate analysis. Collagen content and solubility was determined. Percentage fat was used as a covariant during statistical analyses. Tenderness, residue and collagen solubility of all cuts decreased significantly with animal age. Collagen solubility was the largest discriminant between the three age groups, while animal age had no significant effect on collagen content. Tenderness of primal cuts from the same carcass varied considerably, with collagen content and shear force resistance as the largest discriminants between the cuts. Cuts most representative of total carcass tenderness were M. vastus lateralis, M. semimembranosus, M. gluteobiceps, M. semitendinosus and M. triceps brachii caput longum.     

The comparison of three β-agonists for growth performance,carcass characteristics and meat quality of feedlot cattle

Forty-eight Bonsmara steers were assigned to three treatment groups and one control group consisting of 12 animals each. The control (C) received no β-agonist, while the three treatment groups received zilpaterol (6 ppm) (Z), ractopamine (30 ppm) (R) or clenbuterol (2 ppm) (Cl) for the last thirty days on feed. Growth performance (final 30 days), USDA quality and yield grades and meat quality (shear force, chemical, histological and biochemical) were compared for the three β-agonist and control groups. Animals responded negatively to Cl treatment during initial stages of supplementation, which was evident in lower feed consumption and initial growth rates. For carcass growth and yield, Cl had greater and more efficient growth rates, higher dressed out yields (proportional), lower USDA yield grades, and reduced marbling compared with C (P < 0.05). For meat quality measurements, the M. longissimus (LL) and M. semitendinosus (ST) were sampled. Cl had the greatest effect (P < 0.05) on WBSF, especially on the LL, followed by Z. Variation in tenderness and ageing effects corresponded with variation in calpastatin activity and myofibrillar fragmentation between treatment groups. While zilpaterol and ractopamine are currently the only products registered for cattle in different countries, it seems that zilpaterol has an advantage in carcass growth efficiency and yield without showing any adaptation problems for animals such as experienced by the more aggressive β-agonist clenbuterol.