Texture Changes Associated with Insolubilization of Sarcoplasmic Proteins During Salt‐vinegar Curing of Fish

Toyohara, Masako; Murata, Michihisa; Andô, Masashi; Kubota, Sumihisa; Sakaguchi, Morihiko; Toyohara, Haruhiko

doi:10.1111/j.1365-2621.1999.tb15916.x

Cited by 34 publications

(21 citation statements)

References 14 publications

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“…The bonds with molecular weight of 41,39,and 36 kDa from threadfin bream Sarcoplasmic proteins represent creatine kinase, aldolase and glyceraldehyde‐3‐phosphate dehydrogenase (Yongsawatdigul & Hemung, ). A 94‐kDa band was assumed to be phosphorylase (Toyohara et al ., ). There was no notable change in the SDS‐PAGE patterns of sarcoplasmic proteins from the three groups when heated to 50 °C.…”

Section: Resultsmentioning

confidence: 97%

Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle

Wang

Luo

Shen

2013

Int J of Food Sci Tech

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Thermal stability of sarcoplasmic protein and myofibrillar protein extracted from fresh and frozen common carp was comparatively studied. Total sulphydryl content (SH) in sarcoplasmic protein solution from 5-month frozen carp decreased by 19.43% compared with fresh sample. The SDS-PAGE patterns showed that all the bands of sarcoplasmic protein from frozen-stored samples were almost invisible at 80°C. Myofibrillar protein from fresh sample exhibited lower turbidity and surface hydrophobicity and higher Ca 2+ -ATPase activity and SH content than frozen-stored sample when heated from 20 to 80°C. The Ca 2+ -ATPase activity from fresh (M0), 2 (M2)-and 5 (M5)-month frozen-stored carp was completely lost at 48, 46 and 46°C, respectively. When heated to 80°C, the SH content of myofibrillar solutions in M0, M2 and M5 decreased by 26%, 60% and 70%, respectively. Sarcoplasmic and myofibrillar proteins from frozen carp were more susceptible to aggregate during heating treatment.

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Section: Resultsmentioning

confidence: 97%

Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle

Wang

Luo

Shen

2013

Int J of Food Sci Tech

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show abstract

“…The bonds with molecular weight of 41, 39, and 36 kDa from sarcoplasmic proteins represented creatine kinase, aldolase, and glyceraldehyde‐3‐phosphate dehydrogenase, respectively (Yongsawatdigul and Hemung ). A 94 kDa band was assumed to be phosphorylase (Toyohara and others ). No obvious changes were observed in the sarcoplasmic protein bands of fillets at 4 °C with storage time (Figure (C)).…”

Section: Resultsmentioning

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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“…In other study, in the raw cod (G.morhua) fillets has been observed 0.4% salt. During brining, the salt content of the fillets increased (Toyohara et al 1999). Higher brine concentration caused (p<0.05) dehydration of the fillets, due to the difference in solute concentration between the brine solution and inherent muscle water; water migrated from fish muscle to the high brine solution (Jittinandana et al 2002).…”

Section: Resultsmentioning

confidence: 99%

Detecting the specific parameters that affect the maturation of farmed sea bass (Dicentrarchus labrax) fillets stored in sunflower oil

et al. 2012

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In this study, it was aimed to detect the specific parameters that effect the maturation of farmed sea bass fillets stored in sunflower oil. Sea bass fillets were taken into the pickling solution (2.5% acetic acid and 11% sodium chloride) at 4°C(±1). Fish meat in each group was analysed for the following parameters; pH, moisture%, acetic acid% and NaCl% in the maturation pickling solution and in sunflower oil. At the end of the 90 days storage, there were not any negative situations about the fish in terms of the scientific approach. It was detected that the skinless samples had the less NaCl and acidity values but scaly and scaleless samples had the higher values. Main reasons are: for the scaly and scaleless samples, the skin acted as a barrier in the pickling solution or oil and for scaly samples, scales depart from the skin and defeat the passing of NaCl and acid to the meat. When evaluating this study results, the fillet group samples which contain more salt and acetic acid are thought to be more appropriate for marinating in terms of shelf-life and quality.

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Texture Changes Associated with Insolubilization of Sarcoplasmic Proteins During Salt‐vinegar Curing of Fish

Cited by 34 publications

References 14 publications

Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle

Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle

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

Detecting the specific parameters that affect the maturation of farmed sea bass (Dicentrarchus labrax) fillets stored in sunflower oil

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