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Protein changes in frozen fish

C R C Critical Reviews in Food Science and Nutrition, 1976
Storage of frozen fish brings about a decrease of extractability of myofibrillar proteins. There is also deterioration of the texture and functional properties of the flesh. In model systems, aggregation of myosin, actin, tropomyosin, and whole myofibrils have been described.
Zdzislaw E. Sikorski   +3 more
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Biochemistry of fish antifreeze proteins

The FASEB Journal, 1990
Four distinct macromolecular antifreezes have been isolated and characterized from different marine fish. These include the glycoprotein antifreezes ( M r 2.5‐33 K), which are made up of a repeating tripeptide (Ala‐Ala‐Thr) n with a ...
P L, Davies, C L, Hew
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Antifreeze Proteins of Teleost Fishes

Annual Review of Physiology, 2001
▪ Abstract  Marine teleosts at high latitudes can encounter ice-laden seawater that is approximately 1°C colder than the colligative freezing point of their body fluids. They avoid freezing by producing small antifreeze proteins (AFPs) that adsorb to ice and halt its growth, thereby producing an additional non-colligative lowering of the freezing point.
G L, Fletcher, C L, Hew, P L, Davies
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Protein nutrition in fish: protein/energy ratio and alternative protein sources to fish meal

Journal of Physiology and Biochemistry, 2000
Those interested in the design and manufacture of feeds for intensive fish farming face the basic concern of formulating mixtures for the best yield at the lowest costs. Of the macronutrients in the feed, protein has and continues to receive special consideration because fish present high and specific needs for this constituent.
A, Sanz   +2 more
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Antifreeze Proteins from Fish Bloods

1978
Publisher Summary Glycoproteins of molecular weights isolated from the blood sera of the two Antarctic fishes, Trematomus borchgrevinki and Dissostichus mawsoni, exhibit antifreezing properties in pure H2O or salt solutions. As the melting point is not affected, a hysteresis exists between the freezing and melting temperatures, and the glycoproteins ...
R E, Feeney, Y, Yeh
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Fish antiviral tripartite motif (TRIM) proteins

Fish & Shellfish Immunology, 2019
Tripartite motif (TRIM) family or RBCC proteins comprises characteristic zinc-binding domains (a RING (R), a B-box type 1 (B1) and a B-box type 2 (B2)) and coiled-coil (CC) domain followed by a C-terminus variable domain. There are about 80 different TRIM proteins in human, but more than 200 in zebrafish with several large gene expansions (ftr >70 ...
Langevin, Christelle   +2 more
openaire   +3 more sources

Fish meals, fish components, and fish protein hydrolysates as potential ingredients in pet foods

Journal of Animal Science, 2006
An experiment to determine the chemical composition and protein quality of 13 fish substrates (pollock by-products, n = 5; fish protein hydrolysates, n = 5; and fish meals, n = 3) was conducted. Two of these substrates, salmon protein hydrolysate (SPH) and salmon meal with crushed bones (SMB), were used to determine their palatability as components of ...
J F, Folador   +7 more
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Fish Antifreeze Proteins

2020
Fish antifreeze proteins (APs) including both glycoproteins and small proteins are associated with freezing avoidance in most polar fishes. There are two major types of APs, the antifreeze glycoproteins (AFGPs) found in Antarctic notothenioid fishes and northern cod fishes (gadids) and three other structurally unique small antifreeze proteins (AFPs) in
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Protein metabolism in fishes

Journal of Fisheries Sciences.com, 2008
Proteins are the most necessary nutrients for growth and surviva of fishes. Protein synthesis abilities of fishes are limited. Therefore, the maximum weight gain, wear out tissue renewal and to produce different products (products of protein like hormones, enzimes, intestine epitel cells) are fed by feed which contain their needed ...
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Proteins in Fish Muscle.: II. Colorimetric Estimation of Fish Muscle Protein

Journal of the Fisheries Research Board of Canada, 1950
A simple colorimetric method for protein estimation based on the biuret reaction has been developed. Protein concentrations of 0.1 to 1.2 mg. of nitrogen may be determined rapidly with an error of less than 2 per cent. Only one reagent is required.
openaire   +1 more source

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