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      The effect of aging and muscle type on the quality characteristics and lipid oxidation of lamb meat

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          Abstract

          The research carried out on meat from 45 ram lambs of the Polish merino breed allowed to determine the effect of meat aging and muscle type on physicochemical characteristics and oxidative stability of lipids. Analysis of physicochemical traits (pH, meat color, expressed juice, cooking loss, shear force, moisture, protein, fat and total collagen content) was performed on fresh and meat aged for 14 d in the longissimus lumborum (LL) and gluteus medius (GM) muscles. The meat aging determined all physicochemical characteristics except protein and fat content. More changes in pH and meat color parameters were defined in the GM muscle compared to the LL muscle. The increase in the tenderness of meat expressed as a reduction ( P < 0.05 ) of shear force values was observed in both muscles aged for 14 d. A lower value ( P < 0.05 ) of the shear force, despite the higher content of collagen, was determined in the GM muscle compared to LL. The investigated muscles differed in the degree of lipid peroxidation expressed as thiobarbituric acid-reactive substances (TBARS) in both fresh and aged meat. The TBARS value was lower ( P < 0.05 ) in the LL muscle than in GM. In the longissimus lumborum muscle, the significantly lower content of polyunsaturated fatty acids (PUFAs) and PUFA n-6 has been recorded. The oxidation stability was not influenced by the meat aging.

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          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. Copyright © 2011 Elsevier Ltd. All rights reserved.
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            Eine einfache Methode zur Bestimmung der Wasserbindung im Muskel

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              Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system.

              Tenderness has been repeatedly reported as the most important quality aspect of meat. However, a number of studies have shown that a significant portion of retail meat can be considered tough. As a consequence, a significant consumer segment is willing to pay a premium for guaranteed tender meat. However, apart from measuring the shear force, there is no reliable method to predict tenderness. Most of the branded meat programs therefore attempt to ensure eating quality by controlling some of the factors that affect tenderness. Meat tenderness is determined by the amount and solubility of connective tissue, sarcomere shortening during rigor development, and postmortem proteolysis of myofibrillar and myofibrillar-associated proteins. Given the effect of postmortem proteolysis on the muscle ultrastructure, titin and desmin are likely key substrates that determine meat tenderness. A large number of studies have shown that the calpain proteolytic system plays a central role in postmortem proteolysis and tenderization. In skeletal muscle, the calpain system consists of at least three proteases, μ-calpain, m-calpain and calpain 3, and an inhibitor of μ- and m-calpain, calpastatin. When activated by calcium, the calpains not only degrade subtrates, but also autolyze, leading to loss of activity. m-Calpain does not autolyze in postmortem muscle and is therefore not involved in postmortem tenderization. Results from a number of studies, including a study on calpain 3 knockout mice, have shown that calpain 3 is also not involved in postmortem proteolysis. However, a large number of studies, including a study on μ-calpain knockout mice, have shown that μ-calpain is largely, if not solely, responsible for postmortem tenderization. Research efforts in this area should, therefore, focus on elucidation of regulation of μ-calpain activity in postmortem muscle. Discovering the mechanisms of μ-calpain activity regulation and methods to promote μ-calpain activity should have a dramatic effect on the ability of researchers to develop reliable methods to predict meat tenderness and on the meat industry to produce a consistently tender product.
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                Author and article information

                Contributors
                Journal
                Arch Anim Breed
                Arch. Tierz
                AAB
                Archives Animal Breeding
                Copernicus GmbH
                2363-9822
                04 July 2019
                2019
                : 62
                : 2
                : 383-391
                Affiliations
                [1]Department of Animal Breeding and Production, Warsaw University of Life Sciences-SGGW, Ciszewskiego 8, 02-786 Warsaw, Poland
                Author notes
                [*]Witold Rant ( witold_rant@ 123456sggw.pl )
                Article
                01021829
                10.5194/aab-62-383-2019
                6852877
                b11f7634-c6ed-47a3-a12b-2698ea60c380
                Copyright: © 2019 Witold Rant et al.

                This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this licence, visit https://creativecommons.org/licenses/by/4.0/

                History
                : 21 January 2019
                : 17 June 2019
                Categories
                Original Study

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