Postmortem Changes in .ALPHA.-Actinin and Connectin in Carp and Rainbow Trout Muscles.

Tsuchiya, Hiroyoshi; Kita, S.; Seki, Nobuo

doi:10.2331/suisan.58.793

Cited by 52 publications

(37 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A third strategy is to store intact muscle for a certain period under different conditions and then analyse the degradation of proteins by electrophoretic techniques during the storage (Bonnal et al, 2001;Jasra, Jasra, & Talesara, 2001;Martinez, Friis, & Careche, 2001;Papa, Alvarez, Verrez-Bagnis, Fleurence, & Benyamin, 1996;Tsuchiya, Kita, & Seki, 1992). With this strategy it is not possible to determine the protease or proteases that are responsible for the degradation.…”

Section: Introductionmentioning

confidence: 98%

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

et al. 2011

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 98%

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

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Texture softening was mainly influenced by the autolysis and denaturation of muscle protein during the chilled and frozen storage (Tsuchiya et al, 1992;Benjakul et al, 1997). Textural differences occurred between and within species due to differences in protein structure as muscle fiber diameter and chemical contents and measurement methods (Jonsson et al, 2001).…”

Section: Texture Analysismentioning

confidence: 99%

Quality evaluation of tray-packed tilapia fillets stored at 0C based on sensory, microbiological, biochemical and physical attributes

Liu¹,

Wen²,

Zhong³

et al. 2010

Afr. J. Biotechnol.

View full text Add to dashboard Cite

The quality deterioration of tray-packed tilapia (genetically improved farmed tilapia strain of Oreochromis niloticus) fillets stored at 0°C were studied by integrated evaluations of sensory, microbiological, biochemical and physical analysis, in order to expound the mechanism of fish spoilage and develop the most reliable indicators for quality assessment. The results showed that four quality index as Pseudomonas counts, total volatile basic nitrogen (TVBN), cadaverine (CAD) and K value were highly correlated (r > 0.90) with storage time and sensory acceptability. Protein degradation was visible on SDS-PAGE when microbiological load exceeded 6 log cfu/g. Thiobarbituric acid reactive substances (TBARS) value remained at a very low level throughout the storage, suggesting low lipid oxidation in muscle. Hardness decrease tested by texture machine was consistent with texture softening of fillets in the sensory evaluation. Considering fish freshness and microbiological safety, the shelf life of tilapia fillets stored at 0°C was approximately 10 -12 days.

show abstract

“…800 kDa nebulin, 29) while horse mackerel muscle has ca. 2400 kDa connectin 12) and ca. 580 kDa nebulin.…”

Section: Resultsmentioning

confidence: 99%

“…Protein bands minutely examined by SDS PAGE [8][9][10] have shown that, in very fresh muscle, the amount ofconnectin was greater than that of -connectin, but that -connectin was cleaved from -connectin during storage and myofibril preparation. [11][12][13] Immunohistochemical studies of -and -connectin using antibodies have suggested the location and function by which connectin affects the elasticity in muscle sarcomeres. [14][15][16][17] As for connectin-like protein in invertebrates, Hu et al reported that there was a band of high molecular protein working by SDS PAGE.…”

mentioning

confidence: 99%

Identification of High Molecular Weight Proteins in Squid Muscle by Western Blotting Analysis and Postmortem Rheological Changes

Kasamatsu

Kimura

Kagawa

et al. 2004

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Postmortem Changes in .ALPHA.-Actinin and Connectin in Carp and Rainbow Trout Muscles.

Cited by 52 publications

References 4 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

Quality evaluation of tray-packed tilapia fillets stored at 0C based on sensory, microbiological, biochemical and physical attributes

Identification of High Molecular Weight Proteins in Squid Muscle by Western Blotting Analysis and Postmortem Rheological Changes

Contact Info

Product

Resources

About