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Thierry Astruc - One of the best experts on this subject based on the ideXlab platform.
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Hyperspectral deep ultraviolet autofluorescence of muscle fibers is affected by postmortem changes.
Journal of agricultural and food chemistry, 2015Co-Authors: Caroline Chagnot, Annie Venien, Frédéric Jamme, Matthieu Réfrégiers, Mickael Desvaux, Thierry AstrucAbstract:After slaughter, muscle cells undergo biochemical and physicochemical changes that may affect their autofluorescence characteristics. The autofluorescent response of different rat extensor digitorum longus (EDL) and soleus muscle fiber types was investigated by deep ultraviolet (UV) synchrotron microspectroscopy immediately after animal sacrifice and after 24 h of storage in a moist chamber at 20 °C. The glycogen content decreased from 23 to 18 μmol/g of fresh muscle in 24 h postmortem. Following a 275 nm excitation wavelength, the spectral muscle fiber autofluorescence response showed discrimination depending upon postmortem time (t0 versus t24 h) on both muscles at 346 and 302 nm and, to a lesser extent, at 408 and 325 nm. Taken individually, all fiber types were discriminated but with variable accuracy, with type IIA showing better separation of t0/t24 h than other fiber types. These results suggest the usefulness of the autofluorescent response of muscle cells for rapid Meat-Aging characterization.
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Hyperspectral deep ultraviolet autofluorescence of muscle fibers is affected by postmortem changes
Journal of Agricultural and Food Chemistry, 2015Co-Authors: Caroline Chagnot, Annie Venien, Frédéric Jamme, Matthieu Réfrégiers, Mickael Desvaux, Thierry AstrucAbstract:After slaughter, muscle cells undergo biochemical and physicochemical changes that may affect their autofluorescence characteristics. The autofluorescent response of different rat extensor digitorum longus (EDL) and soleus muscle fiber types was investigated by deep ultraviolet (UV) synchrotron microspectroscopy immediately after animal sacrifice and after 24 h of storage in a moist chamber at 20 degrees C. The glycogen content decreased from 23 to 18 mumol/g of fresh muscle in 24 h postmortem. Following a 275 nm excitation wavelength, the spectral muscle fiber autofluorescence response showed discrimination depending upon postmortem time (t0 versus t24 h) on both muscles at 346 and 302 nm and, to a lesser extent, at 408 and 325 nm. Taken individually, all fiber types were discriminated but with variable accuracy, with type IIA showing better separation of t0/t24 h than other fiber types. These results suggest the usefulness of the autofluorescent response of muscle cells for rapid Meat-Aging characterization.
Lello Zolla - One of the best experts on this subject based on the ideXlab platform.
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proteolysis in Meat tenderization from the point of view of each single protein a proteomic perspective
Journal of Proteomics, 2016Co-Authors: Alessandro Lana, Lello ZollaAbstract:Abstract Muscle has to undergo a number of biochemical changes to become the final product, and, once become Meat, needs to develop the proper organoleptic peculiarities, including tenderness. Tenderness depends on multiple factors, intervening throughout the production chain, from animal's birth till the end of Meat Aging. Given the striking number of variables, it is not an exaggeration to affirm that Meat coming from each individual is a ‘unique’ Meat. So, the process of Meat tenderization follows different paths; Meat derived from different animals shows its own evolution, but underneath the wide variability, all these individual developments follow a standard template: in other words, there are some boundaries that limit the possible variations. This review wants to give a comprehensive idea of the concept of Meat tenderness, in particular focusing on the two protein classes that are among the most important direct responsibles for tenderization: sarcomeric proteins and proteolytic enzymes. We will review the most recent and significant data acquired on each protein, pointing the attention on the results collected by means of the ‘omics’ technologies, and underlining the possible role of markers in the frame of Meat tenderness. Biological significance Our review discusses the evidences collected by means of the ‘omics’ technologies about the proteolytic mechanisms that act in the muscle-to-Meat conversion process, leading the muscle to reach the acceptable tenderness of the eatable Meat. We consider the proteolytic enzymes and their substrate individually, summarizing the most significant data from the omic approach, and discussing their possible role of marker of tenderness.
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Apoptosis in muscle-to-Meat Aging process: The omic witness.
Journal of proteomics, 2015Co-Authors: Valentina Longo, Alessandro Lana, Maria Teresa Bottero, Lello ZollaAbstract:Abstract Meat derives from a muscle that undergoes a great number of biochemical and physiological changes. The anoxic condition established from the moment of animal sacrifice forces muscle cells to a sort of reaction, resulting in methodical programmed cell death to avoid necrosis. The duality autophagy and/or apoptosis is at the center of the scientific debate about the biological processes driving the muscle to Meat conversion. Here we report an omic time course overview carried on proteome, phosphoproteome and metabolome of Piedmontese longissimus thoracis muscle searching for clues helping us to extricate through the dilemma. The survey depicts a progressive physiological impairing and our evidences push towards the apoptotic behavior: the proteomic time course trend of annexin A2, RKIP, HSPB6, αB crystalline, adenylate kinase, DJ-1 and 31 kDa actin fragment; the 0–1 day increased phosphorylation of myosin 2 and synaptopodin and the metabolomic time course trend of key metabolic indicators, like GSH/GSSG ratio, taurine and nitrotyrosine. The employed techniques provide strong indications about the likely apoptotic behavior of Aging Meat in muscle-to-Meat conversion process. Biological significance Our work underlines compelling evidences of the apoptotic behavior of Piedmontese beef muscle cells undergoing the muscle-to-Meat process, whereas no autophagic clues are inferred from this omic investigation.
Edward Pospiech - One of the best experts on this subject based on the ideXlab platform.
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Species-specific expression of various proteins in Meat tissue: proteomic analysis of raw and cooked Meat and Meat products made from beef, pork and selected poultry species.
Food Chemistry, 2012Co-Authors: Magdalena Montowska, Edward PospiechAbstract:The aim was to search for proteins differentiating the six species (cattle, pig, chicken, turkey, duck and goose) and relatively stable during the Meat Aging and only slightly degraded in ready-made products. The two-dimensional electrophoresis was used for analysis of the protein profiles from raw Meat and frankfurters and sausages (15 products). The observed species-specific differences in protein expression in raw Meat were retained in processed products after finishing the entire technological process. Regulatory proteins, metabolic enzymes, some myofibrillar and blood plasma proteins were identified, which were characterised by the electrophoretic mobility specific to the given species. Large differences in the primary structure were observed in serum albumin, apolipoprotein B, HSP27, H-FABP, ATP synthase, cytochrome bc-1 subunit 1 and alpha-ETF. Some of these proteins have potential to be used as markers in authentication of Meat products.
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Differences in two-dimensional gel electrophoresis patterns of skeletal muscle myosin light chain isoforms between Bos taurus, Sus scrofa and selected poultry species.
Journal of the science of food and agriculture, 2011Co-Authors: Magdalena Montowska, Edward PospiechAbstract:BACKGROUND: In this study the interspecies differences in two-dimensional electrophoresis patterns of skeletal muscle myosin light chain (MLC) isoforms between Bos taurus (cattle), Sus scrofa (pig), Gallus gallus (chicken), Meleagris gallopavo (turkey), Anas platyrhynchos (duck) and Anser anser (goose) were characterised on the basis of specific properties of MLCs associated with their structure and mobility in gel. RESULTS: Two-dimensional electrophoresis separations revealed species-specific differences in the molecular weight and pI of individual MLC isoforms (MLC1f, MLC2f and MLC3f). In the case of closely related animal species such as goose and duck or turkey and chicken, significant differences occurred in MLC1f. For MLC2f, differences between cattle and turkey and between pig and chicken were around 1 and 0.3 kDa respectively. It appeared from the comparison of amino acid sequences that even MLCs with only 2% difference in sequences have different electrophoretic mobilities. CONCLUSION: Interspecies differences in skeletal MLC isoforms appeared between cattle, pig, chicken, turkey, duck and goose. The slight changes observed in the course of the Aging process confirmed that these proteins are relatively little susceptible to proteolytic enzymes during Meat Aging. Copyright © 2011 Society of Chemical Industry
Jean-françois Hocquette - One of the best experts on this subject based on the ideXlab platform.
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Proteome changes during Meat Aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef Aging and tenderization.
Journal of agricultural and food chemistry, 2009Co-Authors: Elisabeth Laville, Gilles Renand, Thierry Sayd, Martine Morzel, Sylvie Blinet, Christophe Chambon, Jacques Lepetit, Jean-françois HocquetteAbstract:Within a population of Charolais young bulls, two extreme groups of longissimus thoracis muscle samples, classified according to Warner−Bratzler shear force (WBSF) of 55 °C grilled Meat, were analyzed by 2D-electrophoresis. Muscle analyses were performed on 4 bulls of the “tender” group (WBSF = 27.7 ± 4.8 N) and 4 bulls of the “tough” group (WBSF = 41.2 ± 6.1 N), at 3 post-mortem times: D0, samples taken within 10 min post-mortem; D5 and D21, samples kept at 4 °C under vacuum during 5 and 21 days. Proteins of muscle samples were separated in two fractions based on protein solubility in Tris buffer: “soluble” and “insoluble”. Proteins of both fractions were separated by 2D-electrophoresis. Evolution of spots during the 3 post-mortem times was analyzed by hierarchical classification (HCA). Three clusters of proteins presenting similar evolution profiles provided accurate classification of post-mortem times and showed the translocation of some chaperone proteins and glycolytic enzymes from the soluble fracti...
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New indicators of beef sensory quality revealed by expression of specific genes.
Journal of agricultural and food chemistry, 2007Co-Authors: Carine Bernard, Isabelle Cassar-malek, Martine Le Cunff, Hervé Dubroeucq, Gilles Renand, Jean-françois HocquetteAbstract:To identify new molecular markers of beef sensory quality, the transcriptomes of Longissimus thoracis muscle from 25 Charolais bull calves were analyzed using microarrays and compared between high and low Meat quality groups; 215 genes were differentially expressed according to tenderness, juiciness, and/or flavor. Among these, 23 were up-regulated in the tenderest, juiciest, and tastiest Meats, and 18 were highly correlated with both flavor and juiciness (e.g., PRKAG1), explaining up to 60% of their variability. Nine were down-regulated in the same Meats, but only DNAJA1 [the results relating to DNAJA1 and its relationship with tenderness have been patented (Genomic marker for Meat tenderness; Patent EP06300943.5, September 12, 2006)], which encodes a heat shock protein, showed a strong negative correlation with tenderness that alone explained 63% of its variability. This protein, known for its anti-apoptotic role, could be involved in Meat Aging. Thus, DNAJA1 could constitute a new marker of beef sensory quality.
Caroline Chagnot - One of the best experts on this subject based on the ideXlab platform.
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Hyperspectral deep ultraviolet autofluorescence of muscle fibers is affected by postmortem changes.
Journal of agricultural and food chemistry, 2015Co-Authors: Caroline Chagnot, Annie Venien, Frédéric Jamme, Matthieu Réfrégiers, Mickael Desvaux, Thierry AstrucAbstract:After slaughter, muscle cells undergo biochemical and physicochemical changes that may affect their autofluorescence characteristics. The autofluorescent response of different rat extensor digitorum longus (EDL) and soleus muscle fiber types was investigated by deep ultraviolet (UV) synchrotron microspectroscopy immediately after animal sacrifice and after 24 h of storage in a moist chamber at 20 °C. The glycogen content decreased from 23 to 18 μmol/g of fresh muscle in 24 h postmortem. Following a 275 nm excitation wavelength, the spectral muscle fiber autofluorescence response showed discrimination depending upon postmortem time (t0 versus t24 h) on both muscles at 346 and 302 nm and, to a lesser extent, at 408 and 325 nm. Taken individually, all fiber types were discriminated but with variable accuracy, with type IIA showing better separation of t0/t24 h than other fiber types. These results suggest the usefulness of the autofluorescent response of muscle cells for rapid Meat-Aging characterization.
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Hyperspectral deep ultraviolet autofluorescence of muscle fibers is affected by postmortem changes
Journal of Agricultural and Food Chemistry, 2015Co-Authors: Caroline Chagnot, Annie Venien, Frédéric Jamme, Matthieu Réfrégiers, Mickael Desvaux, Thierry AstrucAbstract:After slaughter, muscle cells undergo biochemical and physicochemical changes that may affect their autofluorescence characteristics. The autofluorescent response of different rat extensor digitorum longus (EDL) and soleus muscle fiber types was investigated by deep ultraviolet (UV) synchrotron microspectroscopy immediately after animal sacrifice and after 24 h of storage in a moist chamber at 20 degrees C. The glycogen content decreased from 23 to 18 mumol/g of fresh muscle in 24 h postmortem. Following a 275 nm excitation wavelength, the spectral muscle fiber autofluorescence response showed discrimination depending upon postmortem time (t0 versus t24 h) on both muscles at 346 and 302 nm and, to a lesser extent, at 408 and 325 nm. Taken individually, all fiber types were discriminated but with variable accuracy, with type IIA showing better separation of t0/t24 h than other fiber types. These results suggest the usefulness of the autofluorescent response of muscle cells for rapid Meat-Aging characterization.