Protease activity higher in postmortem water buffalo meat than Brahman beef

Neath, K.E.; Barrio, Arnel N. Del; Lapitan, Rosalina M.; Herrera, Jesus Rommel V.; Cruz, Libertado C.; Fujihara, Tsutomu; Muroya, Susumu; Chikuni, Koichi; Hirabayashi, Miho; Kanai, Yoshikatsu

doi:10.1016/j.meatsci.2007.04.010

Cited by 20 publications

(14 citation statements)

References 30 publications

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“…Numerous studies have shown that the proteolytic CAPNs activity is responsible for meat tenderization (Sentandreu et al, 2002; Koohmaraie and Geesink, 2006). Therefore, the CAPN system is regarded as the main endogenous protease system contributing to postmortem proteolysis and meat tenderization (Koohmaraie and Geesink, 2006; Bernard et al, 2007; Neath et al, 2007). …”

Section: Introductionmentioning

confidence: 99%

A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review

Lian

Wang²,

Liu³

2013

Asian Australas. J. Anim. Sci

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Tenderness is the most important meat quality trait, which is determined by intracellular environment and extracellular matrix. Particularly, specific protein degradation and protein modification can disrupt the architecture and integrity of muscle cells so that improves the meat tenderness. Endogenous proteolytic systems are responsible for modifying proteinases as well as the meat tenderization. Abundant evidence has testified that calpains (CAPNs) including calpain I (CAPN1) and calpastatin (CAST) have the closest relationship with tenderness in livestock. They are involved in a wide range of physiological processes including muscle growth and differentiation, pathological conditions and post-mortem meat aging. Whereas, Calpain3 (CAPN3) has been established as an important activating enzyme specifically expressed in livestock’s skeletal muscle, but its role in domestic animals meat tenderization remains controversial. In this review, we summarize the role of CAPN1, calpain II (CAPN2) and CAST in post-mortem meat tenderization, and analyse the relationship between CAPN3 and tenderness in domestic animals. Besides, the possible mechanism affecting post-mortem meat aging and improving meat tenderization, and current possible causes responsible for divergence (whether CAPN3 contributes to animal meat tenderization or not) are inferred. Only the possible mechanism of CAPN3 in meat tenderization has been confirmed, while its exact role still needs to be studied further.

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Section: Introductionmentioning

confidence: 99%

A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review

Lian

Wang²,

Liu³

2013

Asian Australas. J. Anim. Sci

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“…The application of Protease Inhibitor Cocktails, AEBS, Aprotinin, Bestatin, E-64, Leupeptin, Pepstatin A, and Calpain inhibitor 1 on buffalo meat has suggested that higher calpain activities are responsible for the increased tenderness of water buffalo meat compared to beef soon after slaughter (Neath et al 2007).…”

Section: Discussionmentioning

confidence: 99%

Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness, and cooking loss of hens during aging

Xiong¹,

ZhanG²,

ZhanG³

et al. 2012

Czech J. Food Sci.

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The potential contribution of mechanical disruption by ultrasonics and endogenous proteolytic enzymes on the tenderisation of hen muscle were investigated. The importance of endogenous enzymes was evaluated using various specific inhibitors. Freshly obtained breast muscles of culled hens, from the 6 groups investigated were treated with different proteolytic enzyme inhibitors and/or ultrasonics, group was treated with different methods, and then stored at 4°C for 0, 1, 3, and 7 days. Shear force decreased by 1.19 kg, and shear force and cooking loss were reduced by 0.69 kg and 4.27%, respectively, in the incorporated group treatment. The calpastatin activity was affected by all treatments except in the Z-DEVD-fmk-treated group, caspase-3 activity decreased in Z-DEVD-fmk-treated group. Therefore, the results suggest that ultrasonics and endogenous proteases contributed to muscle degradation, thereby improving hen meat tenderness and decreasing the cooking loss. Thus muscle degradation, tenderness, and water-retaining properties of hens were improved by a combination of ultrasound and exogenous proteolytic enzyme inhibitors.

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“…However, present investigations suggest that the calpain I (µ) is responsible for the degradation of myofi brils structure and in result for the beginning of meat tenderization [Huff--Lonergan et al, 1996; Koohmaraie et al, 2002;Neath et al, 2007]. The calpain II (m) and other proteases can contribute to further proteolysis in the later period of posthumous ageing [Boehm et al, 1998;Dutaud et al, 2006;Neath et al, 2007].…”

Section: Calpains Or/and Caspases In Tenderization?mentioning

confidence: 92%

“…Similar observations were made in relation to calpastatin. The activity of calpain and calpastatin is correlated with tenderness [Geesink & Koohmaraie, 1999;Neath et al, 2007]. For example, meat of callipyge sheep, which is hard, is characterized by a high level of calpastatin and by a slow degradation of proteins [Geesink & Koohmaraie, 1999].…”

Section: Construction and Functioning Of The System Of Calpainsmentioning

confidence: 99%

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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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Protease activity higher in postmortem water buffalo meat than Brahman beef

Cited by 20 publications

References 30 publications

A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review

A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review

Influence of ultrasound and proteolytic enzyme inhibitors on muscle degradation, tenderness, and cooking loss of hens during aging

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

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