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  • 1
    Electronic Resource
    Electronic Resource
    Inactivity of μ-Calpain Throughout Postmortem Aging of Meat (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), 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: : In order to determine the involvement of μ-calpain in the tenderization of meat during postmortem aging, μ-calpain was prepared from porcine skeletal muscle and its activity was measured under various conditions, using casein and myofibrils as the substrate. μ-Calpain was inactive at pH 5.89 and below 15 °C. Even when the reaction time was extended to 10 h, it was entirely inactive at pH 5.62 and 5 °C. In the early postmortem stage, when the pH value of muscle is above 6.0, μ-calpain was considered to be inactive due to the low concentration of sarcoplasmic calcium ions. μ-Calpain is, therefore, irrelevant to the tenderization of meat throughout postmortem aging.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2002.tb10651.x
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  • 2
    Electronic Resource
    Electronic Resource
    Suppression of Experimental Allergic Neuritis by Cyclosporin A (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 540 (1988), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1988.tb27167.x
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  • 3
    Electronic Resource
    Electronic Resource
    A system for imaging transverse distribution of scattered light and chlorophyll fluorescence in intact rice leaves (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 17 (1994), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In order to examine the transverse distribution of scattered light and chlorophyll fluorescence in intact rice leaves, a micro-fluorescence imaging system was devised using a microscope, a CCD camera with an image intensifier, an Ar and a He-Ne laser light source, an image processor, and a microcomputer. A laser light was projected vertically on to the surface of a rice leaf segment at a cut-edge, and scattered light and induced fluorescence were observed at the cut-section from a 90° angle to the axis of the laser beam. The intensity of scattered light showed a maximum at several micrometres depth from the leaf surface and a steep gradient afterwards. Fluorescence reached a maximum crossing with the decline curve of the scattered light. The maximum of fluorescence measured at 741 nm was observed at a greater depth from the leaf surface than that at 687 nm, suggesting that part of the fluorescence of the longer wavelength was emitted due to absorption of fluorescence of the shorter wavelength. Profiles of the scattered light and the chlorophyll fluorescence depended on leaf anatomy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.1994.tb00271.x
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  • 4
    Electronic Resource
    Electronic Resource
    Soft and Ca-retaining Gelatin Prepared by Conjugating with Acidic Saccharides (2004)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 69 (2004), 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: : Gelatin samples conjugated with acidic saccharides such as glucuronic acid, alginic acid oligosac-charide, and low-molecular-weight alginic acid were prepared to improve the functional properties of ossein gelatin by the Maillard reaction. The conjugation resulted in a decreased isoelectric point, retardate gelation time, low storage modulus, and low melting temperature and enthalpy of gelatin gel; in particular, low-molecular-weight alginic acid resulted in a large improvement. The alginic acid oligosaccharide-conjugated gelatins and low-molecular-weight alginic acid-conjugated gelatins had calcium-retaining ability, and the latter exhibited calcium-aggregating ability. It is thus considered that conjugation with low-molecular-weight alginic acid could be effective for providing a new type of gelatin with a soft texture and calcium-retaining and calcium-aggregating ability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2004.tb10986.x
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  • 5
    Electronic Resource
    Electronic Resource
    Relationship Between Fragmentation of Myofibrils and Liberation of Phospholipids from Z-Disks Induced by Calcium Ions at 0.1 mM: Mechanism of Tenderization of Pork and Beef during Postmortem Aging (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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: We studied the myofibril fragmentation using porcine and bovine myofibrils to determine the mechanism by which myofibrils are fragmented during postmortem aging of meat. Both myofibril fragmentation and liberation of phospholipids from Z-disks were maximally induced by calcium ions at 0.1 mM. These phenomena showed identical dependencies on pH and temperature in the presence of calcium ions at 0.1 mM. All phospholipids in Z-disks, except for lysophosphatidylethanolamine, had affinity for calcium ions. Therefore, we concluded that liberation of calcium-phospholipid compounds from Z-disks causes weakening of the Z-disk structure, resulting in the myofibril fragmentation during postmortem aging of meat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb05780.x
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  • 6
    Electronic Resource
    Electronic Resource
    Relationship Between Weakening of Z-disks and Liberation of Phospholipids During Postmortem Aging of Pork and Beef (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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 liberation of phospholipids from Z-disks was investigated to elucidate the cause of the structural weakening of Z-disks, which contributes to the tenderization of meat during postmortem aging. The amounts of lipids in Z-disks were 2.2 g per 100 g of myofibrillar proteins in porcine and 2.7 g in bovine semitendinosus muscles. Phospholipids were the major component of the lipids. The postmortem liberation of phospholipids correlated well with Z-disk weakening, though a-actinin, the major protein of Z-disks, remained unchanged even after prolonged aging of pork and beef. We therefore concluded that Z-disks are weakened by liberation of phospholipids during postmortem aging of pork and beef.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb14121.x
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  • 7
    Electronic Resource
    Electronic Resource
    Tenderization of Heated Sliced Beef by Succinylated Glycerol Monostearate, a Novel Meat Tenderizer (2001)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), 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: Succinylated glycerol monostearate (SGMS) was most effective in reducing shear-force value when used as a surfactant to tenderize meat using sheep casings as a model of intramuscular connective tissue. Roasted beef slices that had been treated with 2% granular SGMS showed a marked decrease in toughness due to the penetration of SGMS along the perimysium during heating. Collagen fibrils in the perimysium were transformed into a sheet-like structure that seemed very likely to be a complex of SGMS and thermally denatured collagen. These structural changes could account for the tenderness of the roasted beef slices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2001.tb04596.x
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  • 8
    Electronic Resource
    Electronic Resource
    Water/Oil Emulsions Prepared by the Membrane Emulsification Method and Their Stability (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 64 (1999), 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: We developed and tested a simple method to measure dispersed droplet size of W/O emulsions. Then, using a microporous glass membrane treated with oil phase, we produced a W/O emulsion with high water content (40% w/w) at a high emulsification rate by the membrane emulsification method, and assessed its stability. In comparison with emulsions by the stirring methods, variations in dispersed droplet size and viscosity of emulsions by membrane method were small and the emulsions were more stable. Droplet size was not related to the stability of the W/O emulsion prepared by membrane emulsification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb15867.x
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation of Peptides with Angiotensin I-converting Enzyme Inhibitory Effect Derived from Hydrolysate of Upstream Chum Salmon Muscle (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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: In order to utilize upstream chum salmon as a component of nutraceutical food, their defatted muscle proteins were hydrolyzed with 5% thermolysin. The resulting hydrolysate showed high inhibitory activity against angiotensin I-converting enzyme (inhibitory concentration50= 27.9 protein μg/mL) in vitro. A significant reduction of systolic blood pressure was observed when 500 and 2000 mg/kg of body weight were orally administered into spontaneously hypertensive rats. Angiotensin I-converting enzyme inhibitory peptides contained in the hydrolysate were isolated with various chromatographs. These 6 active peptides were Trp residue-containing dipeptides: Trp-Ala, Val-Trp, Trp-Met, Met-Trp, Ile-Trp, and Leu-Trp. The inhibitory concentration50 values of these dipeptides ranged from 2.5 μM to 277.3 μM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb12300.x
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  • 10
    Electronic Resource
    Electronic Resource
    Structural Changes in Titin and Nebulin Filaments Specific to Calcium Ions at 0.1 mM: Factors of Meat Tenderization During Postmortem Aging (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), 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 structural changes in titin and nebulin filaments were investigated by incubating isolated myofibrils in a solution containing 0.1 mM calcium ions and various concentrations of a protease inhibitor. The inhibition curves showed 2 abnormal steps with increases in the concentration of leupeptin or calpastatin domain I. While the amounts of unchanged titin and nebulin were constant in the 1st step, the 2nd occurred at higher protease inhibitor concentrations. These facts indicated that excess amounts of leupeptin and calpastatin domain I caused deterioration in titin and nebulin properties, thus interfering with the binding of calcium ions. We concluded that the severance of titin and nebulin filaments in the 1st step were induced by calcium ions at 0.1 mM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb08237.x
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