## Abstract Natural actomyosin was isolated from cod (__Gadus morhua__ L) stored in ice for up to 28 days. The gelling properties, apparent viscosity, Ca^2β^βATPase activity and component protein composition by sodium dodecyl sulphate (SDS) electrophoresis were determined for each preparation of na
Changes in intramuscular collagen of cod (Gadus morhua) during post-mortem storage in ice
β Scribed by Pilar Montero; Ian M Mackie
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 604 KB
- Volume
- 59
- Category
- Article
- ISSN
- 0022-5142
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β¦ Synopsis
Abstract
Intramuscular collagen was isolated from the muscle of large and small cod (Gadus morhua L) stored in ice for periods up to 24 days. The solubilities in salt solution (salt soluble collagen), in dilute acetic acid (acid soluble collagen) and on heating (heat soluble collagen) were used as indices of aggregation. The solubility of collagen decreased slightly as rigor mortis developed in the flesh, but as rigor resolved it increased markedly. On storage postβrigor the solubilities on heating and in acid increased steadily and coincided with sharp increases in acidic and alkaline proteolytic activity in the muscle. The results obtained indicate that degradation of collagen takes places initially with the development of rigor mortis and that it continues as the muscle ages. Possible mechanisms are discussed.
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## Abstract Content of protein fractions dissolved in 0,5 β 5% NaCl solutions (total protein, myofibrillar protein and crude actomyosin) were investigated in meat tissue of Baltic cod and Baltic herring stored in ice at 1 Β°C (Β±1 Β°C). Cod was showing faster reduction in extractability of soluble pro