Location of and post-mortem changes in some cytoskeletal proteins in pork and cod muscle

Morrison, E. H.; Bremner, H A; Purslow, Peter P.

doi:10.1002/(sici)1097-0010(20000501)80:6<691::aid-jsfa590>3.0.co;2-t

Cited by 16 publications

(9 citation statements)

References 37 publications

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“…Formation of extracellular drip channels has been related to post mortem changes in cytoskeleton and weakening of the integrity of the cod muscle structure and is a time dependant process (Morrison, Bremner & Purslow, 2000). In addition, the strong contraction suggested in the fish salted pre-rigor may have reduced passage through these channels.…”

Section: Mass Transfermentioning

confidence: 99%

Physical and quality attributes of salted cod (Gadus morhua L.) as affected by the state of rigor and freezing prior to salting

Lauritzsen¹,

Akse²,

Johansen³

et al. 2004

Food Research International

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The effects of the rigor state and freezing of cod prior to salting on the mass transfer during production and the quality of heavily cured cod have been investigated. Pre-rigor salting lead to a larger reduction in weight, a higher water loss and a lower uptake of NaCl than in fish salted post-rigor and in fish salted after frozen storage. The cause of this is believed to be the simultaneous influx of NaCl and rigor contractions in the fish muscle. In order to reduce the loss of proteins from the raw material and to increase the instrumental lightness values (L*) of the salt ripened product, the fish should be salted in pre-rigor state.However, if the primary focus is on the weight yield, the fish should be salted post-rigor after chilling or freezing pre-or post-rigor. Freezing and thawing of cod prior to salting post-rigor increased the firmness of the salt cured product compared to chilled fish salted post-rigor.

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Section: Mass Transfermentioning

confidence: 99%

Physical and quality attributes of salted cod (Gadus morhua L.) as affected by the state of rigor and freezing prior to salting

Lauritzsen¹,

Akse²,

Johansen³

et al. 2004

Food Research International

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show abstract

“…Relatively little post mortem degradation occurs in several cytoskeletal proteins in fish compared to mammalian muscle (Verrez-Bagnis 1997;Morrison et al 2000). However, it is the extra-cellular matrix in fish that seems to be more rapidly and easily degraded, due to the rapid breakdown of the abundant type V collagen in myocommata (Ando et al 1991;Sato et al 1994).…”

Section: Introductionmentioning

confidence: 99%

Changes in muscle collagen content during post mortem storage of farmed sea bream (Sparus aurata): influence on textural properties

et al. 2005

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The changes in collagen content and its solubility in sea bream muscle were studied for variable storage times following the death of the fish, and these variables were related to the evolution of physical parameters important for consumer acceptance: firmness and water-holding capacity (WHC). The results show that the collagen content in muscle diminished slightly over storage time and that this variable was directly related to firmness but inversely related to the waterholding capacity. With regard to collagen solubility, a decline was detected in acid-soluble collagen (ASC) in the first few post mortem hours, perhaps related to the end of rigor mortis that occurs at these stages. Pepsin-soluble collagen (PSC) increased, while insoluble collagen (ISC) decreased from 96 h, coinciding with a loss of firmness. This softening can be explained as a result of specific collagenases acting on the insoluble fraction of the collagen.

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“…It appears that this is consistent with breakdown of the extracellular matrix (ECM) 1 -3 and, to a lesser degree, with degradation of intracellular elements. 4,5 Montero and Mackie 6 found that collagen in cod (Gadus morhua) muscle degraded during ice storage of fillets. In Atlantic salmon (Salmo salar) the acid-soluble collagen fraction, specifically type V collagen, appears to increase during storage.…”

Section: Introductionmentioning

confidence: 99%

Gelatinolytic activities in muscle of Atlantic cod (Gadus morhua), spotted wolffish (Anarhichas minor) and Atlantic salmon (Salmo salar)

Lødemel

Olsen

2003

J Sci Food Agric

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The gelatinolytic activity in muscle from Atlantic cod (Gadus morhua), spotted wolffish (Anarhichas minor) and Atlantic salmon (Salmo salar) was studied using gelatin SDS-PAGE, gelatin affinity chromatography and enzyme inhibitors. These fish species are known to differ markedly in fillet softening and gaping post mortem. Atlantic cod, which is a promising species for cold water marine aquaculture, often shows such negative properties, particularly after being well fed. Gelatinolytic activity bands were present in all three species. Using gelatin chromatography and enzyme inhibitors, both serine proteinases and metalloproteinases were detected in wolffish and cod muscle, while only the latter were found in salmon muscle. Activation of the metalloproteinases by p-aminophenylmercuric acetate (APMA) resulted in a shift in activity from higher to lower molecular weight, as is known for mammalian matrix metalloproteinases. In all three species the molecular weight of the metalloproteinases was lowered from approximately 80 to about 70 kDa by activating with APMA.

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Location of and post-mortem changes in some cytoskeletal proteins in pork and cod muscle

Cited by 16 publications

References 37 publications

Physical and quality attributes of salted cod (Gadus morhua L.) as affected by the state of rigor and freezing prior to salting

Physical and quality attributes of salted cod (Gadus morhua L.) as affected by the state of rigor and freezing prior to salting

Changes in muscle collagen content during post mortem storage of farmed sea bream (Sparus aurata): influence on textural properties

Gelatinolytic activities in muscle of Atlantic cod (Gadus morhua), spotted wolffish (Anarhichas minor) and Atlantic salmon (Salmo salar)

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