Effect of prerigor lactic acid treatment on lysosomal enzyme release in bovine muscle

Ertbjerg, Per; Larsen, Lone Melchior; Møller, A.J.

doi:10.1002/(sici)1097-0010(199901)79:1<95::aid-jsfa188>3.0.co;2-f

Cited by 29 publications

(17 citation statements)

References 23 publications

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“…These alterations are similar to the muscle changes reported for the cooked muscle of sea bass, Dicentrarchus labrax L. (Ayala and others 2005), cod ( Gadus morhua L.), and salmon ( Salmo salar ) (Ofstad and others 1996), where heating produced coagulation and denaturation of proteins. Results found in the present study were a consequence of the lowering of the muscle tissue pH and the resulting increase in enzyme activities, especially lysosomes proteinase activities, as reported by other researchers (Etherington 1974; Mason and others 1984; Mikami and others 1987; Ouali 1987; Ertbjer and others 1999b). The cathepsins degrade the muscle components, such as Z lines, actin, myosin, Troponin‐T, and desmin filaments (Ladrat and others 2003; Delbarre‐Ladrat and others 2006).…”

Section: Resultssupporting

confidence: 88%

“…The potential causes for tenderization due to marinating are: pH induced swelling of muscle fibers and/or connective tissue; accelerated or additional proteolytic weakening of muscle structure, and increased solubilization of collagen upon cooking. The lowering of meat pH is also favorable for an increased release and activity of lysosomal cathepsins (Ertbjer and others 1999b). This can cause enhanced potential for proteolysis, as the lysosomal enzymes cathepsin B and L can cleave both myofibrillar proteins (Mikami and others 1987; Ouali 1987) and collagenous proteins (Etherington 1974; Mason and others 1984).…”

Section: Introductionmentioning

confidence: 99%

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Structural Changes in Marinated Fillets of Gilthead Sea Bream (Sparus aurata L.) during Vacuum Storage at Refrigerated Temperature

Ayala¹,

Gil²,

Vázquez³

et al. 2011

Journal of Food Science

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Fillets of Sparus aurata were marinated in a mixture of salt (5.5%) and citric acid (48.9 g/kg) for 1 h, then vacuum packed and refrigerated for 1, 5, 16, and 21 d. Structural and ultrastructural parameters were evaluated in 6 specimens per time period. At day 1, the preservative solution appeared among the muscle fibers, thus increasing the interfibrillar spaces; cytoplasmic organelles were swollen and the sarcolemma-endomysium appeared very altered and electron-dense. At 5 to 10 d, the marinade solution had penetrated into the muscle fibers. The subsarcolemmal and intermyofibrillar spaces were dilated and granular lines of electron-dense material appeared among the fibers. From 16 d, broad interfibrillar spaces were occupied by granular material derived from denatured sarcolemma-endomysium and denatured myofibrils. Sarcomeres were already altered from initial stages, mainly at the I-band level. The Z-line also appeared disrupted. Such alterations were more severe from 10 d on, such that most of the sarcomeres showed disintegration of myofilaments.

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Section: Resultssupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Structural Changes in Marinated Fillets of Gilthead Sea Bream (Sparus aurata L.) during Vacuum Storage at Refrigerated Temperature

Ayala¹,

Gil²,

Vázquez³

et al. 2011

Journal of Food Science

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“…In most of these studies, the enzymes were extracted from the stored muscle before activity determinations. In addition to the presence of inhibitors, cellular compartmentalization may impede the ability of proteolytic enzymes such as the lysosomal proteases, to degrade cellular proteins (Whiting, Montgomery & Anglemier 1975; Ertbjerg, Larsen & Møller 1999; Kubo, Gerelt, Han, Sugiyama, Nishiumi & Suzuki 2002). Using a polyclonal antibody raised against cod liver cathepsin D, we investigated the presence of cathepsin D in the cod fillets during storage and in the collected drip (Fig.…”

Section: Resultsmentioning

confidence: 99%

Pre-rigor filleting and drip loss from fillets of farmed Atlantic cod (Gadus morhua L.)

et al. 2007

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Improved slaughtering procedures of farmed ¢sh may provide su⁄cient time so that ¢lleting can be performed pre-rigor while the muscle pH is still high. Such ¢lleting not only reduces ¢llet gaping but also lowers the transportation costs and makes fresh ¢llets available to the markets at an earlier stage. The aim of our work was to determine the weight reduction of the ¢llets due to liquid loss and to study the proteins and enzymes in the drip. After11days of cold storage, ¢llets of farmed Atlantic cod produced prerigor had a weight loss of 10% and a ¢llet contraction of 19% while for ¢llets produced post-rigor the values were 5% and 4% respectively. At the same time, approximately twice the amount of proteins had been lost from the pre-rigor-produced ¢llets. Sodium dodecyl sulphate polyacrylamide gel electrophoresis analysis showed that the proteins in the drip were similar to the sarcoplasmatic proteins extracted from the muscle. Speci¢c analysis of proteolytic enzymes indicated that they are less stable in the expelled liquid than in the £esh during storage. The extensive loss of weight and proteins from pre-rigor-produced ¢llets during subsequent storage must be taken into account if such processing is considered for farmed cod.

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“…Subcellular fractionation was conducted according to Ertbjerg and others () with some modifications. Muscle samples (0.5 g) were homogenized with 4.5 mL of buffer (100 mM sucrose, 100 mM KCl, 50 mM tris‐HCl, 10 mM sodium pyrophosphate, 1 mM Na 2 EDTA, pH 7.2) and then the homogenate was centrifuged to separate the myofibrillar fraction (1100 g for 20 min), heavy mitochondrial fraction (3000 g for 20 min), lysosomal fraction (16000 g for 30 min) and the remaining supernatant (sarcoplasm).…”

Section: Methodsmentioning

confidence: 99%

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Han

Liu

Zhang

et al. 2015

Journal of Food Science

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To investigate the effects of chilling and partial freezing on rigor mortis changes in bighead carp (Aristichthys nobilis), pH, cathepsin B, cathepsin B+L activities, SDS-PAGE of sarcoplasmic and myofibrillar proteins, texture, and changes in microstructure of fillets at 4 °C and -3 °C were determined at 0, 2, 4, 8, 12, 24, 48, and 72 h after slaughter. The results indicated that pH of fillets (6.50 to 6.80) was appropriate for cathepsin function during the rigor mortis. For fillets that were chilled and partially frozen, the cathepsin activity in lysosome increased consistently during the first 12 h, followed by a decrease from the 12 to 24 h, which paralleled an increase in activity in heavy mitochondria, myofibrils and sarcoplasm. There was no significant difference in cathepsin activity in lysosomes between fillets at 4 °C and -3 °C (P > 0.05). Partially frozen fillets had greater cathepsin activity in heavy mitochondria than chilled samples from the 48 to 72 h. In addition, partially frozen fillets showed higher cathepsin activity in sarcoplasm and lower cathepsin activity in myofibrils compared with chilled fillets. Correspondingly, we observed degradation of α-actinin (105 kDa) by cathepsin L in chilled fillets and degradation of creatine kinase (41 kDa) by cathepsin B in partially frozen fillets during the rigor mortis. The decline of hardness for both fillets might be attributed to the accumulation of cathepsin in myofibrils from the 8 to 24 h. The lower cathepsin activity in myofibrils for fillets that were partially frozen might induce a more intact cytoskeletal structure than fillets that were chilled.

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Effect of prerigor lactic acid treatment on lysosomal enzyme release in bovine muscle

Cited by 29 publications

References 23 publications

Structural Changes in Marinated Fillets of Gilthead Sea Bream (Sparus aurata L.) during Vacuum Storage at Refrigerated Temperature

Structural Changes in Marinated Fillets of Gilthead Sea Bream (Sparus aurata L.) during Vacuum Storage at Refrigerated Temperature

Pre-rigor filleting and drip loss from fillets of farmed Atlantic cod (Gadus morhua L.)

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

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