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  • Blackwell Publishing Ltd  (10)
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  • 1
    Electronic Resource
    Electronic Resource
    Heat-Induced Tendering of Turban Shell (Batillus cornutus) Muscle (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The foot, opercular and visceral muscles were excised from the turban shell Batillus cornutus, and their heat-induced changes in toughness and ultrastructure were compared. When heated up to 30°C, the toughness of foot muscle decreased in the upper and middle regions, but increased in the lower region. The toughness of these three regions decreased at temperatures between 50-70°C, where collagen might be denatured. Some changes in toughness were also observed in the opercular muscle by heating up to 30°C, whereas the toughness of visceral muscle remained unchanged over a wide range of temperature. Transmission electron microscopy showed that the intrinsic structure of collagen fibrils in each muscle was lost at 60°C, with partial swelling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb12994.x
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Storage Temperature on Rigor-Mortis and ATP Degradation in Plaice Paralichthys olivaceus Muscle (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Live specimens of the plaice Paralichthys olivaceus were spiked at the brain, stored at various temperatures ranging from 0° to 20°C and examined for changes in rigor tension and ATP degradation in the muscle. The ATP degradation rate was clearly slower at 5–15°C than at WC, resulting in retardation of rigor- mortis onset at the former temperatures. Lactic acid accumulation in the muscle correlated well with the decrease of ATP. The muscle showed an ATP concentration of 3 μmol/g and “rigor index” (full rigor = 100%) at 30% when lactic acid increased up to 30 μmol/g at most storage temperatures. The muscle showed full rigor when ATP completely disappeared and lactic acid attained the maximum plateau (40–50 μmol/g).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb05867.x
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  • 3
    Electronic Resource
    Electronic Resource
    Temperature-Dependency of Rigor-Mortis of Fish Muscle: Myofibrillar Mg2+-ATPase Activity and Ca2+ Uptake by Sarcoplasmic Reticulum (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Myofibrillar Mg2+-ATPase activity of plaice and red sea bream increased with increase in reaction temperature and Ca2+ concentration. However, temperature decrease tended to lower Ca2+ sensitivity of Mg2+-ATPase activity. While it was assumed that spiked fish muscle was relaxed and the myofibrillar Ca2+ concentration was low, the progress rate of rigor-mortis correlated well with Mg2+-ATPase activity in the presence of a few micromolar Ca2+ at 0°C. Correspondingly, it was found that Ca2+ uptake by plaice sarcoplasmic reticulum decreased with the decrease in reaction temperature. These results strongly suggest the acceleration of fish rigor-mortis at 0°C is due to the increase of Ca2+ concentration in myofibrils during storage at this temperature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1989.tb05933.x
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  • 4
    Electronic Resource
    Electronic Resource
    Postmortem Changes in ATP, Creatine Phosphate, and Lactate in Sardine Muscle (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Postmortem changes were followed in sardines stored in ice. Fast (“white”) muscle creatine phosphate began decreasing from 25 μmol/ g immediately after death. ATP concentration remained about 10 μmol/ g and began decreasing after 2 hr when rigor mortis onset was observed. ATP decreased rapidly when creatine phosphate concentration reached a level similar to ATP, and was 2 μmol/g after 8 hr when full rigor was observed. Lactate accumulation proceeded parallel to ATP degradation (correlation coefficient r = -0.995) and the degree of rigor mortis (r = -0.989). In contrast, sardine slow muscle was low in creatine phosphate (1 μmol/g) and ATP (5 μmol/g), both of which decreased immediately after death. Lactate accumulation was low in this muscle and correlation with rigor mortis progress was lower (r = -0.902) than for fast muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb07998.x
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  • 5
    Electronic Resource
    Electronic Resource
    ATP and Creatine Phosphate Breakdown in Spiked Plaice Muscle during Storage, and Activities of Some Enzymes Involved (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The onset of rigor-mortis of plaice Puralichthys olivaceus spiked at the brain started much faster at 0°C than at 10°C. Correspondingly, ATP and creatine phosphate breakdown and lactic acid accumulation in the muscle were faster at 0°C. ATP concentration was constant at 5 μmol/g until creatine phosphate decreased from the initial conccntration at around 20 μmol/g to 5 μmol/g, irrespective of storage temperature. Simultaneously, lactic acid accumulated, slowly at first, until ATP concentration started decreasing, and then quickly accompanying the full-rigor state. Activities of the enzymes involved in ATP and creatine phosphate consumption-myofibrillar and sarcoplasmic AT-Pases and creatine kinase-were temperature-dependent, and decreased with decrease in temperature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1988.tb07810.x
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  • 6
    Electronic Resource
    Electronic Resource
    Heat-Induced Textural and Histological Changes of Ordinary and Dark Muscles of Yellowfin Tuna (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: When a fresh specimen of yellowfin tuna Neothunnus albacora was analyzed, the cross-sectional area of ordinary (white) muscle fiber was 3.5 times larger than that of dark muscle. As heating temperature was raised, the shear force of dark muscle became progressively larger than that of ordinary muscle. Simultaneously, the A band in the ultrastructure of both muscles was stained more densely. While the Z line in I band of dark muscle still remained, that of ordinary muscle disappeared completely by heat treatment at 60°C for 30 min. Therefore, the differences in toughness change during heat treatment correlated well with that fiber sizes and ultrastructures of the two types of muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1988.tb08929.x
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  • 7
    Electronic Resource
    Electronic Resource
    Acceleration of Physicochemical Change in Carp Muscle by Washing in Either Chilled or Heated Water (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: “Arai” (washing) is a traditional cooking method of fish preparation in Japan. Carp muscle slices were washed in water (49°C for 15 sec, or 0°C for 10 min), and examined for physical and biochemical changes. At 49°C, rigor-mortis was accelerated, resulting in a marked decrease of muscle slice thickness. ATP degradation proceeded faster at 49°C than at 0°C. Arai treatment at 49°C increased myofibrillar Mg2+ - AT-Pase activity 8-9 times in the absence of Ca2+, but did not affect activity in the presence of Ca2+ as much, giving only a 1.2 times increase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb05204.x
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  • 8
    Electronic Resource
    Electronic Resource
    Thermal Degradation of Paralytic Shellfish Poison (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Components of paralytic shellfish poison (PSP) were heated under various conditions, and examined for changes in toxicity and in HPLC and TLC behaviors. The thermal degradation of PSP components progressed as a first order reaction, at different rates depending upon component and temperature. A mixture of gonyautoxin 2 and gonyautoxin 3 when dissolved in water and heated at 100°, 110°, and 120°C (180 min) retained 39, 17, and less than 3%, respectively, of initial toxicity. A mixture of gonyautoxin 1 and gonyautoxin 4 was more therrnolabile; i.e. it retained little toxicity when heated at 120°C for 60 min. HPLC and TLC analyses demonstrated that heating under those conditions converted PSP components into other substances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb08643.x
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  • 9
    Electronic Resource
    Electronic Resource
    Short Thermal Treatment Effect on Carp Myofibril and Sarcoplasmic Reticulum: Possible Mechanisms in Rigor Mortis Acceleration by “Arai” Treatment (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Inorganic γ-phosphate liberation from adenosine 5′-triphosphate (ATP) by carp myofibrillar ATPase was measured at 0-60°C to elucidate mechanisms in rigor mortis acceleration of sliced carp muscle during washing at a moderately high temperature. ATP splitting within 20 sec in the presence of 5 mM MgCl2 plus 0.25 mM CaCl2 was maximal at 45°C, which agreed well with the commercially adopted condition for preparing carp “arai” muscle. In addition, the maximum Ca2+ uptake by sarcoplasmic reticulum was observed at 30°C and decreased at higher temperatures. The acceleration of carp muscle rigor mortis at around 45°C was suggested to be partly due to enhancement of myofibrillar Mg2+-ATPase activity by increase of intracellular Ca2+ concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb05349.x
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  • 10
    Electronic Resource
    Electronic Resource
    Autoxidation of Bluefin Tuna Myoglobin Associated with Freezing and Thawing (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Bluefin tuna oxymyoglobin (oxyMb) solutions were frozen either quickly at −80°C or slowly at −2O°C, thawed, and the metmyoglobin (metMb) to total myoglobin (Mb) ratio (metMb%) determined. When quick freezing was applied, autoxidation was clearly pH-dependent, with a minimum (metMb%, 15–40) at around pH 5.9–6.3. When slowly frozen and thawed, on the other hand, tuna Mb generally showed an extremely high metMb%. Freezing and thawing partially insolubilized tuna Mb, depending upon pH. The Mb showed the minimum ratio of insolubilization at pH 6–6.3 again. Insolubilization of tuna Mb was markedly accelerated by NaCl.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb06681.x
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