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An associate editor of the journal has experienced an increase in the number of received reviews where the comments to either the authors or to the editor do not align with the reviewer's recommendation to accept, revise or reject. In particular, some recommendations for outright rejection of a submission have been accompanied by criticisms that clearly could have been solved by revision of the manuscript. The purpose of this letter is to provide some guidance to reviewers on the specific issue of deciding between a recommendation to revise versus reject.

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The color of fresh pork is a crucial quality attribute that significantly influences consumer perception and purchase decisions. This review first explores consumer expectations and discrimination regarding pork color, as well as an overview of the underlying factors that, from farm-to-fork, contribute to its variation. Understanding the husbandry factors, peri- and post-mortem factors and consumer preferences is essential for the pork industry to meet market demands effectively. This review then delves into current knowledge of pork myoglobin chemistry, its modifications and pork discoloration. Pork myoglobin, which has certain peculiarities comparted to other meat species, plays a weak role in determining pork color, and a thorough understanding of the biochemical changes it undergoes is crucial to understand and improve color stability. Furthermore, the growing role of proteomics as a high-throughput approach and its application as a powerful research tool in meat research, mainly to decipher the biochemical mechanisms involved in pork color determination and identify protein biomarkers, are highlighted. Based on an integrative muscle biology approach, the available proteomics studies on pork color have enabled us to provide the first repertoire of pork color biomarkers, to shortlist and propose a list of proteins for evaluation, and to provide valuable insights into the interconnected biochemical processes implicated in pork color determination. By highlighting the contributions of proteomics in elucidating the biochemical mechanisms underlying pork color determination, the knowledge gained hold significant potential for the pork industry to effectively meet market demands, enhance product quality, and ensure consistent and appealing pork color.

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The effects of ultrasound (0, 300 and 600 W for 20 min at the frequency of 20 kHz) followed by postmortem aging (0, 4 and 8 d aging time) on beef quality were evaluated. Ultrasound treatment, aging time and their interaction all significantly affected the pH and tenderness of beef (p < 0.05). Furthermore, ultrasound improved the cathepsin B + L activities and the solubility of collagen compared with the control without ultrasound treatment (p < 0.05). In terms of microstructure, the perimysium was ruptured by the ultrasound treatment which caused the collagen fibers to be disorderly and loosely arranged. In addition, ultrasound could affect the structural stability of collagen resulting in a significant reduction of thermal denaturation temperature (p < 0.05). The results showed that ultrasound could improve beef tenderness during postmortem aging by changing collagen structure and regulating the activities of cathepsin B + L.

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Following a century of major discoveries on the mechanisms determining meat colour and tenderness using traditional scientific methods, further research into complex and interactive factors contributing to variations in meat quality is increasingly being based on data-driven "omics" approaches such as proteomics. Using two recent meta-analyses of proteomics studies on beef colour and tenderness, this review examines how knowledge of the mechanisms and factors underlying variations in these meat qualities can be both confirmed and extended by data-driven approaches. While proteomics seems to overlook some sources of variations in beef toughness, it highlights the role of post-mortem energy metabolism in setting the conditions for development of meat colour and tenderness, and also points to the complex interplay of energy metabolism, calcium regulation and mitochondrial metabolism. In using proteomics as a future tool for explaining variations in meat quality, the need for confirmation by further hypothesis-driven experimental studies of post-hoc explanations of why certain proteins are biomarkers of beef quality in data-driven studies is emphasised.

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Over the last two decades, proteomics have been employed to decipher the underlying factors contributing to variation in the quality of muscle foods, including beef tenderness. One such approach is the application of high-throughput protein analytical platforms in the identification of meat quality biomarkers. To broaden our understanding about the biological mechanisms underpinning meat tenderization across a large number of studies, an integromics study was performed to review the current status of protein biomarker discovery targeting beef tenderness. This meta-analysis is the first to gather and propose a comprehensive list of 124 putative protein biomarkers derived from 28 independent proteomics-based experiments, from which 33 robust candidates were identified worthy of evaluation using targeted or untargeted data-independent acquisition proteomic methods. We further provide an overview of the interconnectedness of the main biological pathways impacting tenderness determination after multistep analyses including Gene Ontology annotations, pathway and process enrichment and literature mining, and specifically discuss the major proteins and pathways most often reported in proteomics research.

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Meat color is important for consumer acceptability, with excessively dark meat often associated with consumer rejection. It is determined chromatically by pigment content (measured by hue and chroma) and achromatically by scattering of light by the microstructure (measured by lightness), the latter of which has received minimal research focus. This review discusses the individual components of the meat microstructure that cause differences in achromatic contributions to color. Differences in achromatic light scattering between light and dark extremes of meat color are most likely explained by structural attributes within the muscle cell. These differences are proposed to arise from variations in (a) transverse shrinkage of the structural lattice of the myofilaments, myofibrils, and muscles fibers, (b) longitudinal shrinkage of the sarcomere, and (c) different protein composition of the surrounding medium (sarcoplasm and extracellular space). These are discussed at a mechanistic level, in relation to six parameters of the muscle cell: (a) protein surface charge altering the myofilament spacing, (b) protein solubility, (c) sarcoplasmic protein binding to myofilaments and myofibrils, (d) integrity of the cytoskeleton and cell adhesion proteins, (e) sarcomere integrity and myofibrillar proteins, and (f) myosin denaturation and rigor bond modification. New data are presented to support the proposed role of structural elements in muscle causing achromatic light scattering and their contribution to the surface color of meat. In addition, the relationships between lightness and water holding capacity and pH are explored and the economic impact of dark meat for the meat industry is discussed.

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Extracellular matrix (ECM) structures within skeletal muscle play an important, but under-appreciated, role in muscle development, function and adaptation. Each individual muscle is surrounded by epimysial connective tissue and within the muscle there are two distinct extracellular matrix (ECM) structures, the perimysium and endomysium. Together, these three ECM structures make up the intramuscular connective tissue (IMCT). There are large variations in the amount and composition of IMCT between functionally different muscles. Although IMCT acts as a scaffold for muscle fiber development and growth and acts as a carrier for blood vessels and nerves to the muscle cells, the variability in IMCT between different muscles points to a role in the variations in active and passive mechanical properties of muscles. Some traditional measures of the contribution of endomysial IMCT to passive muscle elasticity relied upon tensile measurements on single fiber preparations. These types of measurements may now be thought to be missing the important point that endomysial IMCT networks within a muscle fascicle coordinate forces and displacements between adjacent muscle cells by shear and that active contractile forces can be transmitted by this route (myofascial force transmission). The amount and geometry of the perimysial ECM network separating muscle fascicles varies more between different muscle than does the amount of endomysium. While there is some evidence for myofascial force transmission between fascicles via the perimysium, the variations in this ECM network appears to be linked to the amount of shear displacements between fascicles that must necessarily occur when the whole muscle contracts and changes shape. Fast growth of muscle by fiber hypertrophy is not always associated with a high turnover of ECM components, but slower rates of growth and muscle wasting may be associated with IMCT remodeling. A hypothesis arising from this observation is that the level of cell signaling via shear between integrin and dystroglycan linkages on the surface of the muscle cells and the overlying endomysium may be the controlling factor for IMCT turnover, although this idea is yet to be tested.

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This review focuses on the mechanisms responsible for some the achromatic aspects of meat colour (paleness or darkness) due to light scatter from structures within the tissue. Recent investigations have highlighted the role of three key mechanisms contributing to variations in the lightness of meat: (1) Variations in the myofilament lattice spacing, and the resultant changes in myofibril diameter and muscle fibre diameter. A 20% increase in lightness (L* value) between muscles with ultimate pH of 6.1 versus 5.4 is accompanied by a 17% change in muscle fibre diameter. (2) Variations in sarcomere length, if these are associated with changes in myofilament and myofiber diameter, (3) Variations in sarcoplasmic protein distribution, including whether these are bound or precipitated onto the myofilaments, as demonstrated by an increase of 1.24 in the ratio of X-ray diffraction intensities from mass centered on the thin filaments versus thick filaments in dark (pH 6.15) versus light (pH 5.47) muscles. For clarity, the discussion of these mechanisms is principally in relation to pH and temperature at rigor (5 °C-35 °C), although the possibility of contributions from numerous other factors is acknowledged.

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El aluminio puede ser consumido por personas a través de la contaminación de alimentos y el agua. Los metales pesa­dos en alimentos de origen animal son un riesgo potencial para la salud de los consumidores. En algunos países, es una práctica habitual que las comidas cocinadas listas para el consumo se presenten y mantengan calientes en bandejas de aluminio en tiendas minoristas, como locales de comida rápida y supermercados. No hay información disponible sobre el desprendimiento de metal en este tipo de recipiente de conservación de alimentos. El objetivo de este estudio fue determinar la concentración de aluminio en la carne y en los líquidos de cocción almacenados en bandejas de aluminio descartables. El diseño del estudio incluyó carne bovina cocida almacenada sola, en una salsa acuosa de hierbas a pH 7, y en una salsa acuosa cítrica (a base de limón) a pH 4, para simular condiciones encontradas en la práctica minorista. El Comité Mixto FAO / OMS de Expertos en Aditivos Alimentarios estableció una ingesta semanal tolerable provisional de 2 mg Al kg-1 de peso corporal. Una sola porción de 250 g de carne en salsa ácida almace­nada en una bandeja de aluminio calentada durante 1, 2, 4 u 8 horas contribuiría con 0,9%, 3,4%, 6,9% y 19,8% respectivamente de acuerdo al límite tolerable. Aunque la carne se mantiene caliente durante largos períodos en bandejas de aluminio descartable, el contenido de aluminio no se acerca a los límites actualmente recomendados. Este estudio proporciona datos que sugieren que puede ser prudente limitar el consumo de este tipo de comidas a base de carne con salsas ácidas almacenadas calientes por tiem­pos extendidos en contenedores de aluminio.

Aluminium can be consumed by people through contamination of foods and in water. Heavy metals in foods of animal origin are a potential risk to the health of consumers. It is common practice in some countries that ready-to-eat cooked meals are often presented and maintained hot in aluminium trays in retail outlets such as fast food take-out stores and supermarkets. There are not available information about the detachment of metal in this kind of container food preservation. The objective of this study was to determine the concentration of aluminium in meat and cooking liquids stored in disposable aluminium trays. The design of the study included cooked beef meat stored either alone, or in an aqueous sauce of herbs at pH 7, or in a citric (base of lemon) aqueous sauce at pH 4, to simulate a range of conditions found in retail practice. The Joint FAO/WHO Expert Committee on Food Additives established a provisional tolerable weekly intake of 2 mg Al kg body weight-1. A single 250 g portion of meat in acid sauce stored in a heated aluminium tray for 1, 2, 4, or 8 hours would contribute 0.9%, 3.4%, 6.9% or 19.8% towards this tolerable limit, respectively. Although the aluminium content in meat held warm for long periods in aluminium foil trays does not approach the consumption limits currently recommended, this study provides data that suggest that is may be prudent to limit consumption of ready-to eat meat-based meals with acid sauces stored warm in aluminium containers for extended times.

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Long-time low-temperature (LTLT) cooking of meat is known to produce a tender product. The current work tested the hypothesis that LTLT cooking for periods of up to 24 h at 60 °C reduces the contribution of intramuscular connective tissue to cooked meat toughness. Tensile tests on perimysium excised after cooking showed that its strength diminished with cooking time, although not as markedly as the Warner-Bratzler peak force measure of toughness. A gradually increasing susceptibility to trypsin digestion with increasing heating time demonstrated that there was a slow and gradual increase in the proportion of denatured collagen in the perimysium. Differential scanning calorimetry on perimysium excised after cooking showed an endothermic peak representing the denaturation of the collagen not already denatured on cooking. With increasing cooking time, the energy per milligram of collagen necessary to denature this remaining fraction increased. These results support the hypothesis that there is both an easily destabilized and more resistant fractions of the collagen in intramuscular connective tissue.

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Connective tissues such as tendon, ligament and skin are biological fibre composites comprising collagen fibrils reinforcing the weak proteoglycan-rich ground substance in extracellular matrix (ECM). One of the hallmarks of ageing of connective tissues is the progressive and irreversible change in the tissue mechanical properties; this is often attributed to the underlying changes to the collagen fibril structure. This dataset represents a comprehensive screen of the mechanical properties and collagen fibril structure of tendon from the tails of young to old (i.e. 1.6-35.3 month-old) C57BL6/B mice. The mechanical portion consists of the load-displacement data, as well as the derived tensile properties; the structure data consists of transmission electron micrographs of collagen fibril cross section, as well as the derived cross-sectional parameters. This dataset will allow other researchers to develop and demonstrate the utility of innovative multiscale models and approaches of the extra-cellular and physiological events of ageing of current interest to ageing research, by reducing the current reliance on conducting new mammalian experiments.

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Variations in the quantity and thermal stability of collagen in intramuscular connective tissue (IMCT) play a role in variations in cooked meat tenderness. This review is focussed on sources of variability, especially in the perimysial IMCT, and challenges some of the accepted ideas about its denaturation behaviour, its contribution to cooking shrinkage at high temperatures and the concept of IMCT as an immutable "background toughness". IMCT dominates the shear strength of raw and lightly cooked muscle, but at cooking temperatures of 70-80° its contribution is smaller than the myofibrillar component. The thermal denaturation temperature of IMCT collagen given by differential scanning calorimetry at fast heating rates is usually in the range of 62-67 °C, but collagen denaturation is a multistep, non-equilibrium process that is highly heating-rate dependent and can occur at 55-60 °C in slow heating regimes, such as slow roasting or sous-vide cooking. Although it is commonly assumed that collagen shrinkage drives shrinkage of meat and greater cooking losses above 65 °C, an examination of currently available information suggested that there is no evidence to support this idea. The amount and thermal stability of IMCT collagen can be varied by factors manipulating growth rate, and a recent model of these effects is discussed. The characteristics of the thermally-stable fraction of IMCT collagen as the most important component influencing the connective tissue contribution to cooked meat toughness and the need for future work investigating mechanisms to degrade or turnover this specific fraction is suggested.

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The thermal denaturation of collagen the perimysium of intramuscular connective tissue isolated from bovine Semitendinosus (ST) and Perctoralis profundus (PP) muscles was investigated using a range of heating rates in differential scanning calorimetry (DSC) and analyzed by application of the Kissinger-Akahira-Sunose (KAS) and Lumry-Eyring models. Thermograms showed a broadening of endotherms and a shift towards higher temperatures as the thermal scanning rate increased. These features are consistent with the two-step process of a reversible transition between native and unfolded collagen molecules followed by an irreversible transition between unfolded and denatured states. There were small differences between muscles in the onset temperatures of the thermal transitions at heating rates of 0.5 K min-1, while both the KAS and Lumry-Eyring models yielded similar values for the effective activation energy of the whole two-step process, the Lumry-Eyring model allowed a greater insight into differences in the reversible and irreversible steps between the perimysium both muscles. Reversible unwinding of the triple-helical collagen molecules in the perimysium from ST muscle required more energy than in PP muscle. It is speculated that the presence of large amounts of elastin in the perimysium of ST muscles may influence this due to a protein crowding mechanism, or by affecting the covalent cross-linking of the collagen.

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Differences in the thermal shrinkage and collagen solubility between bovine Semitendinosus (ST) and Pectoralis profundus (PP) muscles and their interactions with ageing were evaluated by studying collagen solubility, hydrothermal isometric tension and thermal denaturation properties of intramuscular connective tissue after 5-20days post-mortem storage at 4°C. Collagen solubility was higher in ST than in PP muscle at 5-13days, but the differences between the two muscles decreased at longer ageing times. A small decrease in the peak denaturation temperature of perimysium occurred with increasing ageing times in both muscles. Maximum force in isometrically-heated perimysium was broadly equivalent in both muscles. Although the amount and solubility of collagen varies between muscles and ageing decreases the stability of some of the collagen, thermal shrinkage forces in heated perimysium are not significantly diminished by ageing. These findings support the idea of one collagen fraction easily degraded by ageing and heat, and another more resistant fraction that determines the physical properties of the tissue after ageing and cooking.

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Matrix metalloproteinases (MMPs) are a group of enzymes that degrade extracellular matrix components but are also important signaling molecules that regulate many biological processes including muscle, adipose and connective tissue development. Most recently it has been discovered that MMPs act as intracellular signaling molecules inducing gene expression and altering related proteins in the nucleus. Several single nucleotide polymorphisms of MMPs and their inhibitors are known to exist and most of the research on MMPs to date has focused on their activity in relation to human health and disease. Nevertheless there is a growing body of evidence identifying important roles of MMPs as regulators of myogenesis, fibrogenesis and adipogenesis. The aim of this review is to highlight the currently known functions of the MMPs that have a direct bearing on the deposition of meat components and their relationship with meat quality. Some central pathways by which these enzymes can affect the tenderness, the amount and type of fatty acids are highlighted.

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Oat ß-glucan consumption is linked to reduced risk factors associated with diabetes and obesity by lowering glycemic response and serum level of low-density lipoproteins. The purpose of this study was to identify the mechanism of action of oat ß-glucan at the interface between the gut wall and the lumen responsible for attenuating glucose levels. We proposed that viscous oat ß-glucan acts as a physical barrier to glucose uptake in normally absorptive gut epithelial cells IEC-6 by affecting the expression of intestinal glucose transporters. Concentration and time-dependent changes in glucose uptake were established by using a nonmetabolizable glucose analog 2-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]-2-deoxy-d-glucose. The effectiveness of nutrient transport in IEC-6 cells was shown by significant differences in glucose uptake and corresponding transporter expression. The expressions of glucose transporters sodium-glucose-linked transport protein 1 (SGLT1) and glucose transporter 2 (GLUT2) increased with time (0-60 minutes) and glucose levels (5-25 mmol/L). The suppression of glucose uptake and SGLT1 and GLUT2 expression by increasing concentrations (4-8 mg/mL) of oat ß-glucan demonstrated a direct effect of the physical properties of oat ß-glucan on glucose transport. These results affirmed oat ß-glucan as a dietary agent for minimizing postprandial glucose and showed that modulating the activity of the key intestinal glucose transporters with oat ß-glucan could be an effective way of lowering blood glucose levels in patients with diabetes.

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The heat-solubility of intramuscular collagen is usually conducted in 1/4 Ringer's solution at pH7.4, despite this ionic strength and pH being inappropriate for post-rigor meat. The current work studied the percentage of soluble collagen and hydrothermal isometric tension characteristics of perimysial strips on bovine semitendinosus muscles in either 1/4 Ringer's solution, distilled water, PBS, or a solution of the same salt concentration as 1/4 Ringer's but at pH5.6. Values of % soluble collagen were lower at pH7.4 than 5.6. Increasing ionic strength reduced % soluble collagen. The maximum perimysial isometric tension was independent of the bathing medium, but the percent relaxation was higher at pH7.4 than at pH5.6, and increased with ionic strength of the media. It is recommended that future measurements of collagen solubility and tests on connective tissue components of post-rigor meat should be carried out in a solution of concentrations NaCl and KCl equivalent to those in 1/4 Ringer's, but at pH5.6, a pH relevant to post-rigor meat.

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Intramuscular connective tissue (IMCT) forms a series of continuous networks integrating muscle fibers and fascicles into a whole organ. The contributions of IMCT to cooked meat toughness have long been recognized. This review concentrates on (a) the potential to manipulate IMCT in the growing animal, (b) postmortem effects on structure and properties of IMCT, and (c) developments in techniques to quantify IMCT in meat. A new hypothesis can explain why IMCT is enzymatically degraded in postmortem aging; however, after cooking, no differences are seen in the IMCT contribution to toughness. This hypothesis proposes that heat-insoluble collagen occurs in a weak pool and a strong pool, where the weak pool is most easily degraded by both proteolysis and heat. Far from being a constant background feature, the IMCT contribution to cooked meat toughness can be varied and deserves fresh research on how to achieve this.

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