Modelling post-mortem tenderisation—I: Texture of electrically stimulated and non-stimulated beef

Dransfield, Eric; Wakefield, Diane K.; Parkman, I.D.

doi:10.1016/0309-1740(92)90072-c

Cited by 54 publications

(14 citation statements)

References 23 publications

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“…The effect of the calpain system on tenderisation post-slaughter relies on a balance between the rate of activation and activity, and the rate of inactivation or denaturation of the proteolytic enzymes (Dransfield, 1992;Dransfield, 1993;Dransfield, 1994;Dransfield, Etherington & Taylor, 1992;Dransfield, Wakefield & Parkman, 1992).…”

mentioning

confidence: 99%

Genetic and environmental effects on meat quality

Warner¹,

et al. 2010

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In order for livestock industries to consistently produce high quality meat, there must be an understanding of the factors that cause quality to vary, as well as the contribution of genetics. A brief overview of meat tenderness is presented to understand how genotype and environment may interact to influence this trait.Essentially, meat tenderness is determined from the contribution of connective tissue, sarcomere length determined pre-rigor and rate of proteolysis during ageing, as well as contributions from intramuscular fat and post-mortem energy metabolism. The influence of mutations in myostatin, the callipyge gene, the Carwell or ribe eye muscle gene as well as the calpain system on meat tenderness is presented. Specific examples of interactions between the production or processing environment and genetics are presented for both sheep and cattle. The day-to-day variation in tenderness is evident across experiments and this variation needs to be controlled in order to consistently produce tender meat.

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mentioning

confidence: 99%

Genetic and environmental effects on meat quality

Warner¹,

et al. 2010

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“…The fi rst mechanism of tenderization was proposed by Dransfi eld [1992aDransfi eld [ , c, 1994a. According to this author, the calpain I in meat after slaughter is inactive due to a low concentration of calcium ions which in the sarcoplasm reaches as few as 10 -7 mol.…”

Section: Construction and Functioning Of The System Of Calpainsmentioning

confidence: 99%

“…Activation of the calpain I occurs around 6 hours after slaughter (pH around 6.1-6.3) as a result of calcium ions concentration increase in the sarcoplasm to the value of 10 -4 mol. The increase of calcium ions concentration in the sarcoplasm takes place through the activation of the calcium pumps or through the proteolytic attack on the sarcoplasmic reticulum [Dransfi eld, 1992a[Dransfi eld, ,c, 1994a.…”

Section: Construction and Functioning Of The System Of Calpainsmentioning

confidence: 99%

Enzymes in Tenderization of Meat – The System of Calpains and Other Systems

Nowak¹

2011

Pol. J. Food Nutr. Sci.

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These changes lead to obtaining the fi nal meat tenderness.Many studies have shown that tenderness is dependent on such enzymes as: cathepsins and calpains. Some researchers suggest that proteasomes may be responsible for the fi nal tenderness, while others that caspases [Bernard et al., 2007;Kemp et al., 2010]. However, many studies have assigned this role to the calpains system [Neth et al., 2007;Kemp et al., 2010]. Therefore, in this paper most attention is dedicated to calpains. This paper includes the characteristics of calpains as well as their localization, structure, activity of calpain system, and research in this fi eld. Recently, genetic tests have provided much information. Markers are used commercially to assess meat quality. At present, we are observing great interest in the caspases which may contribute to postmortem proteolysis and tenderization of meat. This paper mentions this fact as well. ENZYMES IN TENDERIZATIONThe mechanism of meat tenderization is complicated. Numerous investigations are being conducted which are aimed at explaining the mechanism of meat tenderization and factors responsible for the initiation and course of this process. There are theories of enzymatic and non-enzymatic meat tenderization. Many studies have shown that enzymes (proteases) are responsible for tenderization. It is considered that the protease system can be involved in postmortem proteolysis and meat Tenderness of meat is considered as the most important feature of meat quality. Three proteolytic systems present in a muscle were examined as those which can play a role in the postmortem proteolysis and tenderization: the system of calpains, lysosomal cathepsins and MCP (multicatalytic proteinase complex). There are several theories (enzymatic or non-enzymatic) explaining the tenderization process. The calpain theory of tenderization was recognized as the most probable. During tenderization the main structures of a cytoskeleton are degraded as well as myofi bril and cytoskeletal proteins. Meat becomes soft and the process of tenderization is accompanied by changes in the ultrastructure (degradation of the Z-line and the I-band). Many studies show that the system of calpains (especially calpain I and calpastatin) plays a major role in postmortem proteolysis and meat tenderization. However, recent studies show that proteasomes and caspases may be responsible for this process as well. This paper includes the characterization of calpains as well as describes the construction and functioning of the system of calpains. Additionally, this article presents factors infl uencing the activity of calpains. It was also mentioned that other systems, such as proteasomes and caspases, may be involved in postmortem tenderization of meat.

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“…These include electrical stimulation (Dransfield et al, 1992;Simmons et al, 2008), carcass suspension (Sørheim & Hildrum, 2002) and muscle stretching (Toohey et al, 2012a;b), natural ageing (Lawrie, 1998), blade tenderisation (Benito- Delgado et al, 1994;Pietrasik & Shand, 2011), marination (Scanga et al, 2000), injection (McGee et al, 2003) and explosion (Solomon et al, 1997). Meat-enhancing agents such as phosphates and salts have been investigated and their successes have been documented (Kerth et al, 1995;Morris et al, 1997;Holmer et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Physical and chemical properties of selected beef muscles infused with a phosphate and lactate blend

Hoffman¹,

Vermaak²,

Müller³

2012

SA J. An. Sci.

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________________________________________________________________________________ AbstractThe consumer demands a beef product of consistent and acceptable tenderness. The infusion of beef muscles with a blend containing sodium and potassium salts, various phosphates and lactates has the potential to improve the current status of low meat consumption and inconsistent tenderness of fresh beef products in South Africa. In the present investigation, the biceps femoris (BF, silverside), rectus femoris muscle (RF), semitendinosus muscle (ST, eye of the silverside), supraspinatus muscle (SS, scotch fillet) and longissimus et lumborum muscles from the left side of beef carcasses were infused, 3 d post mortem, with a blend consisting of various sodium and potassium salts, di-and triphosphates and lactates, while the corresponding muscles from the right side were untreated and served as the control. The changes in beef quality over a 19-d period and the initial proximate and mineral composition of the muscles were also determined. The general findings suggest that an increase in tenderness concurrent with an acceptable beef colour resulted from the infusion with this blend. The chemical composition of the treated muscles was not negatively affected by the infusion and the mineral content of the treated muscles was increased, accordingly._______________________________________________________________________________

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Modelling post-mortem tenderisation—I: Texture of electrically stimulated and non-stimulated beef

Cited by 54 publications

References 23 publications

Genetic and environmental effects on meat quality

Genetic and environmental effects on meat quality

Enzymes in Tenderization of Meat – The System of Calpains and Other Systems

Physical and chemical properties of selected beef muscles infused with a phosphate and lactate blend

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