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Tenderization, meat

Different enzymes have different specificities. Some, such as amylase, are specific for a single substrate, but others operate on a range of substrates. Papain, for instance, a globular protein of 212 amino acids isolated from papaya fruit, catalyzes the hydrolysis of many kinds of peptide bonds. In fact, it s this ability to hydrolyze peptide bonds that makes papain useful as a meat tenderizer and a cleaner for contact lenses. [Pg.1041]

Tenderness. The contractile state of the muscle after rigor mortis is a major factor in meat tenderness, which is affected by post-mortem conditions creating differences in tenderness. Ageing of fresh pork can be used to improve tenderness. The process is based on a continuous weakening of the structural elements by different endogenous muscle peptidases along with an improved palatability (Taylor et al., 1995). [Pg.154]

Papain is a cysteine protease isolated from the latex of the immature fruit and leaves of the plant Carica papaya. It consists of a single 23.4 kDa, 212 amino acid polypeptide, and the purified enzyme exhibits broad proteolytic activity. Although it can be used as a debriding agent, it is also used for a variety of other industrial processes, including meat tenderizing and for the clarification of beverages. [Pg.364]

Avoid high-tyramine foods cheese (aged), sour cream, beer, wine, pickled products, liver, raisins, bananas, figs, avocados, meat tenderizers, chocolate,yogurt soy... [Pg.648]

The cascade of biochemical events described above enhances the cellular necrosis and tissue breakdown, leading to what meat scientists and food technologist call meat-tenderization. Since muscle is primarily protein in nature and since hydrolytic, and specifically proteolytic, activity increases during postmortem aging, muscle represents a remarkable pool of material for the production of flavor peptides and amino acids as well as other precursors for flavor development (2). [Pg.79]

Papain, the active component of most meat tenderizes, is a proteolytic enzyme. [Pg.1137]

Papain—a plant protease derived from the papaya fruit. The enzyme is used in digestive aids, wound debridement, tooth-cleaning and. most importantly, as a meat tenderizer. [Pg.306]

Degradation of proteins by proteases has important implications for the quality of many foods. These include beneficial effects in the development of desirable attributes, such as texture and flavor, e.g. in cheese manufacturing, meat tenderization, beer brewing, soy and fish sauce manufacturing, and production of protein hydrolysates of various origins for different functional or nutritional purposes. The proteases involved may be endogenous to the foods or they may be added for specific pur-... [Pg.354]

Voisey, P.W. 1976. Engineering assessment and critique of instruments used for meat tenderness evaluation. J. Texture Studies 7 11-48. [Pg.1183]

Voisey, P.W. and Larmond, E. (1977). The effect of deformation rate on the relationship between sensory and instrumental measurements of meat tenderness by the Warner- Bratzler method. Canad. Inst. Food Sci. Technol. 10, 307-312. [Pg.324]

Papain Hydrolysis of proteins Papaya fruit (Carica Meat tenderizer ... [Pg.420]

Crude papaya latex, usually called papain, has found a number of industrial applications. It has been used in brewing, meat tenderization, flavor production. [Pg.118]

The use of papain in meat tenderization [70] is almost completely restricted to the United States. A number of techniques have been described (preslaughter as well as post slaughter administration) but are not always very successful. In all cases, papain action does not occur before the cooking of the meat and therefore the result is influenced by many factors other than the actual method of application. It has also been aiguedthat the use of papain in meat tenderizes, toothpaste, beer, and fruit juices is the main reason for the higher incidence of systemic allergic reactions after injection of chymopapain for treatment of sciatica in North America than in Europe. [Pg.118]

Proteolytic (protein-cleaving) enzymes also have applications in consumer products. For example, papain (from papaya extract) serves as a meat tenderizer. It cleaves the fibrous proteins, making the meat less tough. [Pg.1182]

Meat tenderness has been measured with the shear press. This can be done with the 10-blade universal cell or with the single-... [Pg.228]

A pressure method for measuring meat tenderness has been described by Sperring et al. (1959). A sample of raw meat is contained in a cylinder that has a small hole in its bottom. A hydraulic press forces a plunger into the cylinder, and the pressure required to squeeze the meat through the hole is taken as a measure of tenderness. [Pg.229]

A meat grinder technique for measuring meat tenderness was reported by Miyada and Tappel (1956) in this method, power consumption of the meat grinder motor was used as a measure of meat tenderness. The electronic recording food grinder described by Voisey and deMan (1970) measures the torque exerted on a strain gage transducer. This apparatus has been used successfully for measuring meat tenderness. [Pg.229]

Other methods used for meat tenderness evaluation have included measurement of sarcomere length (Howard and Judge 1968) and determination of the amount of connective tissue present. [Pg.229]

Voisey, P.W., and H. Hansen. 1967. A shear apparatus Wehrli, H.P., and Y. Pomeranz. 1969. The role of for meat tenderness evaluation. Food Technol. 21 chemical bonds in dough. Bakers Digest 43 no. 6 ... [Pg.247]

Meat Tenderizing. This is the second largest use of papain. About one-third of all the papain sold in this country is used by the housewife... [Pg.203]


See other pages where Tenderization, meat is mentioned: [Pg.439]    [Pg.32]    [Pg.76]    [Pg.135]    [Pg.76]    [Pg.175]    [Pg.71]    [Pg.161]    [Pg.229]    [Pg.11]    [Pg.49]    [Pg.630]    [Pg.200]    [Pg.406]    [Pg.118]    [Pg.55]    [Pg.73]    [Pg.226]    [Pg.1182]    [Pg.228]    [Pg.229]    [Pg.4]    [Pg.29]    [Pg.204]    [Pg.372]    [Pg.654]   
See also in sourсe #XX -- [ Pg.118 ]

See also in sourсe #XX -- [ Pg.98 ]

See also in sourсe #XX -- [ Pg.21 , Pg.57 ]




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