Influence of lamb age and high-oxygen modified atmosphere packaging on protein polymerization of long-term aged lamb loins

Kim, Yuan H. Brad; Bødker, Sabina; Rosenvold, Katja

doi:10.1016/j.foodchem.2012.04.109

Cited by 26 publications

(15 citation statements)

References 19 publications

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“…An overview of the literature on the relationship between oxidative conditions and textural properties of meat with focus on oxygen in packaging is summarized in Table 1 and studies on meat model systems using either chemical oxidation such as the Fenton reaction or irradiation is summarized in Table 2. Although a few of these studies did not find a significant toughening effect due to oxidation, the consensus is that oxidative conditions, such as high oxygen MAP and irradiation, generally lead to decreased tenderness or increased shear force of meat, as observed in beef (Kim et al 2010;Lagerstedt, Lundström, and Lindahl 2011), pork (Bao and Ertbjerg 2015;Lund et al 2007), lamb (Bórnez et al 2010;Kim et al 2012), and chicken (Yoon, 2003). Some of the studies found that the toughening effect depends on animal species , animal age (Kim et al 2012), or muscle type (Kim et al 2010).…”

Section: Oxidation-induced Meat Tougheningmentioning

confidence: 99%

Effects of protein oxidation on the texture and water-holding of meat: a review

Bao

Ertbjerg

2018

Critical Reviews in Food Science and Nutrition

150

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Protein oxidation readily occurs in postmortem muscle during storage and processing. Over the past decade new analytical methods have been developed and new aspects of protein oxidation in meat have been studied, such as the reaction mechanism, and impacts on eating quality and nutritional value. It is now evident that amino acid side chains in myofibrillar proteins undergoes modifications due to oxidative stress. In turn this will lead to formation of new protein-protein cross-links in structural proteins, however, also the overall level of fixed-charge groups attached to the peptide backbones is modified. Meat texture and water-holding are important quality attributes and they are affected by the oxidation of structural proteins. Different mechanisms have been suggested to explain the oxidation-induced quality changes, focusing mainly on reduced proteolysis and formation of cross-links. This review explores the current understanding of protein oxidation in fresh meat in relation to texture and water-holding. The consequences of protein oxidation at molecular level in relation to oxidation-induced cross-linking and changes in net charges of myofibrillar proteins, and the impacts on texture and water-holding are discussed.

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Section: Oxidation-induced Meat Tougheningmentioning

confidence: 99%

Effects of protein oxidation on the texture and water-holding of meat: a review

Bao

Ertbjerg

2018

Critical Reviews in Food Science and Nutrition

150

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“…These structural changes can induce conformational and functional modifications of proteins including protein solubility (Nieto, Jongberg, Andersen & Skibsted, 2013;Xiong, 2000;Decker, Xiong, Calvert, Crum & Blanchard, 1993), rehydration properties (Nieto et al, 2013;Xiong, 2000), protein fragmentation and aggregation (Promeyrat, Sayd, Laville, Chambon, Lebret & Gatellier, 2011;Santé-Lhoutellier, Astruc, Marinova, Grève & Gatellier, 2008c;Decker et al, 1993), protein surface hydrophobicity (Traore, Aubry, Gatellier, Przybylski, Jaworska, KajakSiemaszko & Santé-Lhoutellier, 2012;Santé-Lhoutellier et al, 2008c), viscosity, gelation and emulsification (Nieto et al, 2013;Xiong, 2000), and amino acid bioavailability (Santé-Lhoutellier et al, 2008c). It is also thought to negatively impact meat color (Filgueras, Gatellier, Lonergan & Huff-Lonergan, 2004a, b) and tenderness (Kim, Bødker & Rosenvold, 2012;Zakrys-Waliwander, O'Sullivan, O'Neill & Kerry, 2012;Lund, Lametsch, Hviid, Jensen & Skibsted, 2007;Melody, Lonergan, Rowe, Huiatt, Mayes & Huff-Lonergan, 2004;Rowe et al, 2004a, b) and decrease water holding capacity (Melody et al, 2004;Decker et al, 1993). …”

Section: Accepted Manuscriptmentioning

confidence: 99%

Development of microbial spoilage and lipid and protein oxidation in rabbit meat

et al. 2015

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This experiment aimed to determine microbial spoilage and lipid and protein oxidation during aerobic refrigerated (4°C) storage of rabbit meat. Forty male New Zealand white rabbits were slaughtered according to the Halal slaughter procedure. The hind limbs were used for microbial analysis while the Longissimus lumborum m. was used for determination of lipid and protein oxidation. Bacterial counts generally increased with aging time and the limit for fresh meat (10(8)cfu/g) was reached at d 7 postmortem. Significant differences in malondialdehyde content were observed after 3d of storage. The thiol concentration significantly decreased with increase in aging time. The band intensities of myosin heavy chain and troponin T significantly reduced with increased refrigerated storage while actin remained relatively stable. This study thus proposes protein oxidation as a potential deteriorative change in refrigerated rabbit meat along with microbial spoilage and lipid oxidation.

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“…Moreover, a significant correlation (r = 0.940, P < 0.05) between the formation of carbonyl groups in myofibrillar proteins and the increase in hardness of superchilled mackerel fillets during storage confirmed this hypothesis. It is generally agreed that oxidative modifications of proteins often lead to a decreased tenderness of both fish and meat (Lund et al, 2008;Kim et al, 2012;Listrat et al, 2016). According to these studies, the toughening effect is often accompanied by formation of protein crosslinks, including collagen crosslinks (Montero & Borderias, 1990;Kim et al, 2012;Listrat et al, 2016), as well as formaldehyde production in the muscle and the aggregation of myofibrillar protein and stroma (Montero & Borderias,1990).…”

Section: Texture Parametersmentioning

confidence: 99%

Superchilled, chilled and frozen storage of Atlantic mackerel (Scomber scombrus) fillets – changes in texture, drip loss, protein solubility and oxidation

Cropotova

Mozūraitytė

Standal

et al. 2019

Int J of Food Sci Tech

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Summary Changes in quality characteristics in relation to protease activity and protein oxidation in chilled, superchilled and frozen mackerel fillets during storage were studied. The solubility of sarcoplasmic proteins was quite stable in mackerel samples for all storage experiments, whereas the solubility of myofibrillar proteins decreased in both superchilled and frozen samples. A significant correlation (r = 0.983, P < 0.05) between the increased activity of cathepsin B+L in chilled fillets and softening of the fish flesh during storage was revealed. Contrary with chilled samples, the texture of superchilled mackerel fillets became tougher along the storage period, which can be explained by a higher rate of myofibrillar oxidation (r = 0.940, P < 0.05). The hardness and drip loss decreased slightly at the end of frozen storage. Superchilling preserved the quality of mackerel fillets with the least side effects in relation to protein solubility, drip loss and softening of the fish tissue as compared to chilled and frozen storage.

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Influence of lamb age and high-oxygen modified atmosphere packaging on protein polymerization of long-term aged lamb loins

Cited by 26 publications

References 19 publications

Effects of protein oxidation on the texture and water-holding of meat: a review

Effects of protein oxidation on the texture and water-holding of meat: a review

Development of microbial spoilage and lipid and protein oxidation in rabbit meat

Superchilled, chilled and frozen storage of Atlantic mackerel (Scomber scombrus) fillets – changes in texture, drip loss, protein solubility and oxidation

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