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

Abstract

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.

The normalisation ofCAPNgene expression inM. pectoralis superficialisin broiler lines differing in growth rate and their relationship to breast muscle tenderness

“…Calpain activity is specifically related to proteolysis of myofibrils and affects post-mortem meat maturation. During post-mortem meat maturation, the proteins comprising the main structure of the cytoskeleton are degraded (Nowak, 2011). Calpain 1 encoded by the CAPN1 gene is mostly situated and active in the Z-line and the remaining 20% in I-bands (Koohmaraie, 1994), while calpain 3 (encoded by CAPN3) is located in the sarcomere near the Z-and M-line of muscle fibres (Ilian et al, 2004).…”

Bromelain: an overview of industrial application and purification strategies

“…Many approaches have been employed to improve postmortem tenderness, including blade tenderization (Pietrasik et al 2010;Pietrasik and Shand 2011), moisture enhancement technology (Streiter et al 2012), and enzymatic treatment (Gerelt et al 2000;Pietrasik and Shand 2011). In a traditional tenderization method, meat is kept cool for up to 10 days to allow postmortem proteolysis by proteolytic enzymes: cathepsins and calpains (Nowak 2011). The potential of proteolytic enzymes such as bromelain, papain, and ficin has been recognized, as shown by their long history of use in meat tenderization.…”

Manfaat Bromelin dari Ekstrak Buah Nanas (Ananas comosus L. Merr) dan Waktu Pemasakan untuk Meningkatkan Kualitas Daging Itik Afkir

“…Bromelin ekstrak buah nanas menghidrolisis jaringan ikat protein daging diantaranya kolagen daging (Illanes, 2008), sehingga dapat membuka struktur mikro daging dengan terputusnya miofibril (Nowak, 2011). Pengujian susut masak menggunakan metode pemasakan yang mengakibatkan terjadinya gap cairan daging dan cairan tersebut dapat tereksudasi keluar mikro struktur daging (Soeparno, 2005), sehingga terjadi penurunan nilai susut masak pada daging.…”