Myosin heavy chain degradation during post mortem storage of Atlantic cod (Gadus morhua L.)

Wang, Pål Anders; Martı́nez, Iciar; Olsen, Ragnar L.

doi:10.1016/j.foodchem.2009.01.031

Cited by 24 publications

(22 citation statements)

References 34 publications

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“…Very little degradation of MHC appeared to have occurred during the 120 h of post-rigor storage at the near neutral pH, indicating that enzymes with such a pH optimum are not of major importance for this breakdown. We have previously shown that degradation of MHC in isolated myofibrils was similarly dependent on pH (Wang et al, 2009). Myosin has isoelectric point at pH 5.5 (Foegeding et al, 1996) and it is known that proteins may be more susceptible to degradation at pH close to the protein's isoelectric point (Dice & Goldberg, 1975).…”

Section: Discussionmentioning

confidence: 95%

“…Sub-cellular compartments are disrupted, enzyme-inhibitor complexes may be formed or dissociated and enzyme precursors may be activated. It is well known that myofibrillar proteins (surimi) obtained after homogenisation and washing of fish muscle possess proteolytic enzyme activities (An, Weerasinghe, Seymour, & Morrissey, 1994;Cao, Jiang, Zhong, Zhang, & Su, 2006;Hu, Morioka, & Itoh, 2008;Wang, Martinez, & Olsen, 2009). It is however an open question if these activities are native to the myofibrillar proteins or if enzyme-myofibrillar complexes are formed during the preparation of the myofibrillar fraction.…”

Section: Introductionmentioning

confidence: 99%

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Post-mortem degradation of myosin heavy chain in intact fish muscle: Effects of pH and enzyme inhibitors

et al. 2011

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a b s t r a c tFish muscle is rapidly degraded during post-mortem storage, due to proteolytic enzymes acting probably both on muscle cells and connective tissue. In this work we have developed a model system which may be used to study the enzymatic degradation occurring in intact post-mortem fish muscle. Degradation of myosin heavy chain (MHC) was monitored in muscle with pH adjusted to 6.05, 6.3 and 6.9 and in the presence of the enzyme inhibitors PMSF, EDTA, phenanthroline, pepstatin A, antipain, E-64 and the cysteine proteinase activator dithiothreithol (DTT). After storage, myofibrillar proteins were isolated and MHC-specific antibodies used to study the degradation in the different samples. MHC from muscle with pH 6.05 and 6.3 was degraded, while no severe degradation was observed at pH 6.9. Introduction of enzyme inhibitors into the muscle tissue clearly showed that mainly cysteine and aspartic proteinases are responsible for the in situ MHC degradation. This is supported by the severe breakdown of MHC in the muscle samples containing DTT.

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Section: Discussionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Post-mortem degradation of myosin heavy chain in intact fish muscle: Effects of pH and enzyme inhibitors

et al. 2011

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“…k a is the first-order rate constant (slope) for each regression analysis of integration of cathepsin activity through 28 days and shear force effectively quantified the contribution of cathepsins to texture deterioration of grass carp fillets. And the results emphasised the detrimental effects of cathepsin B and L. Also, cathepsin D has been suggested not be one of the major proteases associated with postmortem quality deterioration of fish muscle, especially myofibrillar heavy chain (Wang et al, 2009;Ahmed et al, 2013). However, in an in vitro analysis concerning rainbow trout, cathepsin D had been proved to result in changes of more proteins that were related to softening of muscle than cathepsin B and L (Godiksen et al, 2009).…”

Section: Relationship Between Softening Of Grass Carp Fillets and Catmentioning

confidence: 99%

The function of endogenous cathepsin in quality deterioration of grass carp (Ctenopharyngodon idella) fillets stored in chilling conditions

Xia

2014

Int J of Food Sci Tech

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Summary Changes of textural properties and cathepsin activity of grass carp fillets during storage in superchilling (−1.5 ± 0.2 °C) and ice (0.2 ± 0.1 °C) was investigated, and the function of cathepsin in quality deterioration of grass carp fillets was discussed. Results showed that shear force of superchilled and ice‐stored fillets decreased by 50% and 55% after 6 days of storage, respectively. The cathepsin activies in different fractions changed significantly during storage at both conditions. Cathepsin B, B+L activities in sarcoplasma, myofibrillar and heavy mitochondrial fraction significantly increased during the early 3 days postmortem, accompanied by remarkable reduction of corresponding activity in lysosome. Cathepsin D activity in sarcoplasma and myofibrillar significantly increased during 6 days of storage with corresponding decrease in lysosome and heavy mitochondria. Correlation analysis showed that changes of shear force of grass carp fillets were significantly correlated with integration of cathepsin B, D and B+L throughout storage time (r2 > 0.94). As derived from the first‐order exponential decay model, the enzyme efficiencies (ka) of cathepsin B and B+L were more than twofold higher than those of cathepsin D, suggesting the major role of cathepsin B and B+L in textural deterioration of grass carp fillets in chilling storage.

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“…These results indicate that the under‐sides have a stronger degradation than the upper‐sides which may have been influenced by the existence of blood during storage. The degradation of MHC of bled cod muscle in 120–200 kDa became visible after 5 days due to the influence of Cathepsin D during storage at 6°C, but no band was observed below 75 kDa (Wang et al, ). The same results in the SCD groups were observed in our study.…”

Section: Resultsmentioning

confidence: 99%

“…Fish muscle and tissues are composed of structures like myofibrillar (Hayes & Flower, 2013) and collagen proteins (Xu et al, 2015). Myofibrillar proteins occupy the main components which are crucial for maintaining the integrity of texture and mechanical properties of the muscle (Wang, Wartinez, & Olsen, 2009). A transmission electron microscope was used to observe the delay in degradation of pericellular collagen fibrils in six species of bled fishes (yellowtail, horse mackerel, striped jack, red sea bream, flatfish and rudder-fish; Ando et al, 1999).…”

Section: Sds-page and Western-blot In Scd And Sa Groupmentioning

confidence: 99%

Effect of blood deposition phenomenon on flesh quality of yellowtail (Seriola quinqueradiata) during storage

Jiang

Miyazaki

Hirasaka

et al. 2019

Journal of Texture Studies

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We examined the influence of blood deposition on flesh quality of ordinary muscle in yellowtail. This study compared the flesh quality changes in upper and under‐sides of yellowtails killed by two different methods: spinal‐cord destruction (SCD) with blood removal and suffocation in air without blood removal (SA). The under‐sides of the SA group showed the highest values for a*, cathepsin B and B + L activities, the lowest value in breaking strength and the greatest degradation of myosin heavy chain (MHC) among the four groups. However, the values of the SCD‐upper group indicated the best flesh quality. In addition, the white blood cells presented the highest cathepsin B and B + L activities among the blood components. These results indicate that blood has the tendency to deposit downward in accordance with the direction of placement. This phenomenon influences the distribution of white blood cells which contain enzymes that accelerate the deterioration of flesh quality. The texture of fish muscle is an important part of the flesh quality. In captured fishery (purse‐seine fishery and dragnet fishery), it is impossible to immediately and completely remove blood. Therefore, suffocation in air is the common method after the fish is caught. The commercial value of fish is decreased and the price varies greatly when these fish enter market circulation. In our study, we examined the influence of blood deposition on the flesh quality of yellowtail during storage. The degradation of structural proteins accelerated in the deposited blood which contain proteases. The movement and deposition of blood caused the difference of quality on both sides, which seriously affected the quality of fish during preservation. Our study has some theoretical guidance for muscle softening and give a better understanding of the adverse effect of blood during preservation.

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Myosin heavy chain degradation during post mortem storage of Atlantic cod (Gadus morhua L.)

Cited by 24 publications

References 34 publications

Post-mortem degradation of myosin heavy chain in intact fish muscle: Effects of pH and enzyme inhibitors

Post-mortem degradation of myosin heavy chain in intact fish muscle: Effects of pH and enzyme inhibitors

The function of endogenous cathepsin in quality deterioration of grass carp (Ctenopharyngodon idella) fillets stored in chilling conditions

Effect of blood deposition phenomenon on flesh quality of yellowtail (Seriola quinqueradiata) during storage

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