1992
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Proteolytic and physicocohemical mechanisms involved in meat texture development
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Cited by 125 publications
(74 citation statements)
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Abstract
Smart CitationsHow this paper cites the one you are viewing
“…These findings are in accord with the report of Stolowski et al (2006). Furthermore, changes in muscle characteristics, such as muscle bundle size, muscle types, and pH, have been reported to be associated with tenderness (Cross et al, 1973;Ouali, 1992;Maltin et al, 1997). For example, the proteolytic systems (such as calpain -calpastatin system), soluble collagen content, pH, and perimysium thickness are affected by muscle type and breed (Brooks and Savell, 2004;Stolowski et al, 2006;Lefaucheur, 2010).…”
Section: Adjusted Shear Force
supporting
confidence: 88%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…These findings are in accord with the report of Stolowski et al (2006). Furthermore, changes in muscle characteristics, such as muscle bundle size, muscle types, and pH, have been reported to be associated with tenderness (Cross et al, 1973;Ouali, 1992;Maltin et al, 1997). For example, the proteolytic systems (such as calpain -calpastatin system), soluble collagen content, pH, and perimysium thickness are affected by muscle type and breed (Brooks and Savell, 2004;Stolowski et al, 2006;Lefaucheur, 2010).…”
Section: Adjusted Shear Force
supporting
confidence: 88%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…They are also consistent with reports correlating free cathepsin activity, especially that of cathepsins B, L and H, with meat tenderness from 1 d post mortem until the end of the ageing period (Calkins and Seidman 1988;O'Halloran et al 1997). Ouali (1992) suggested that a synergistic action of calpains, cathepsins and proteasomes be considered since all the structural changes identified in post mortem muscle cannot be explained by the action of one proteolytic system. In the post mortem period, the pH of yak meat dropped from 6.84 to 5.54 and later increased to 5.68.…”
Section: Effect Of Ageing Time On Cathepsins Activity
supporting
confidence: 77%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Independently of the genotypes analyzed, the relative area of both 30-and 32-kDa bands increased significantly by freezing. These bands would correspond to troponin-T degradation products (Ouali 1992;Ho et al 1994;Ojeda et al 2001). Therefore, the increase in both 30-and 32-kDa components observed in the present work suggests that proteolytic activity was affected by freezing.…”
Section: Sds-page Analysis Of Myofibril and Sarcoplasmic Proteins
supporting
confidence: 51%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…These findings are in accord with the report of Stolowski et al (2006). Furthermore, changes in muscle characteristics, such as muscle bundle size, muscle types, and pH, have been reported to be associated with tenderness (Cross et al, 1973;Ouali, 1992;Maltin et al, 1997). For example, the proteolytic systems (such as calpain -calpastatin system), soluble collagen content, pH, and perimysium thickness are affected by muscle type and breed (Brooks and Savell, 2004;Stolowski et al, 2006;Lefaucheur, 2010).…”
Section: Adjusted Shear Force
supporting
confidence: 88%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…They are also consistent with reports correlating free cathepsin activity, especially that of cathepsins B, L and H, with meat tenderness from 1 d post mortem until the end of the ageing period (Calkins and Seidman 1988;O'Halloran et al 1997). Ouali (1992) suggested that a synergistic action of calpains, cathepsins and proteasomes be considered since all the structural changes identified in post mortem muscle cannot be explained by the action of one proteolytic system. In the post mortem period, the pH of yak meat dropped from 6.84 to 5.54 and later increased to 5.68.…”
Section: Effect Of Ageing Time On Cathepsins Activity
supporting
confidence: 77%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Independently of the genotypes analyzed, the relative area of both 30-and 32-kDa bands increased significantly by freezing. These bands would correspond to troponin-T degradation products (Ouali 1992;Ho et al 1994;Ojeda et al 2001). Therefore, the increase in both 30-and 32-kDa components observed in the present work suggests that proteolytic activity was affected by freezing.…”
Section: Sds-page Analysis Of Myofibril and Sarcoplasmic Proteins
supporting
confidence: 51%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…These findings are in accord with the report of Stolowski et al (2006). Furthermore, changes in muscle characteristics, such as muscle bundle size, muscle types, and pH, have been reported to be associated with tenderness (Cross et al, 1973;Ouali, 1992;Maltin et al, 1997). For example, the proteolytic systems (such as calpain -calpastatin system), soluble collagen content, pH, and perimysium thickness are affected by muscle type and breed (Brooks and Savell, 2004;Stolowski et al, 2006;Lefaucheur, 2010).…”
Section: Adjusted Shear Force
supporting
confidence: 88%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…They are also consistent with reports correlating free cathepsin activity, especially that of cathepsins B, L and H, with meat tenderness from 1 d post mortem until the end of the ageing period (Calkins and Seidman 1988;O'Halloran et al 1997). Ouali (1992) suggested that a synergistic action of calpains, cathepsins and proteasomes be considered since all the structural changes identified in post mortem muscle cannot be explained by the action of one proteolytic system. In the post mortem period, the pH of yak meat dropped from 6.84 to 5.54 and later increased to 5.68.…”
Section: Effect Of Ageing Time On Cathepsins Activity
supporting
confidence: 77%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…Independently of the genotypes analyzed, the relative area of both 30-and 32-kDa bands increased significantly by freezing. These bands would correspond to troponin-T degradation products (Ouali 1992;Ho et al 1994;Ojeda et al 2001). Therefore, the increase in both 30-and 32-kDa components observed in the present work suggests that proteolytic activity was affected by freezing.…”
Section: Sds-page Analysis Of Myofibril and Sarcoplasmic Proteins
supporting
confidence: 51%