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  • 1
    Electronic Resource
    Electronic Resource
    Thermally Induced Gelation of Selected Comminuted Muscle Systems–Rheological Changes during Processing, Final Strengths and Microstructure (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 49 (1984), 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: Sols were prepared from comminuted fish (surimi), beef, pork and turkey muscles. Continuous evaluation of changes in structural rigidity and energy damping during heating of the sols from 3° to 95°C was performed in a nondestructive, temperature-controlled Thermal Scanning Rigidity Monitor. Surimi presented major rigidity transitions at 40°. 48° and 65°C; beef at 43°. 56° and 69°C; pork at 44°, 53° and 69°C; and turkey at 50°, 53° and 79°C. All materials exhibited rapid decrease in energy damping (i.e. increase in elasticity) over a short temperature span. Failure testing of gels indicated differences in strength and deformability. SEM micrographs provided an insight into structural features of the gels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1984.tb12830.x
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  • 2
    Electronic Resource
    Electronic Resource
    Thermally Induced Gelation of Native and Modified Egg White-Rheological Changes During Processing; Final Strengths and Microstructures (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 49 (1984), 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 heat-induced gelation of native egg white (EW) and egg white modified with succinic anhydride (SEW) or oleic acid (OEW), by addition of 15 moles of reagent/50000g protein, was evaluated. Rigidity modulus (G) and mechanical energy damping were continuously monitored during heating of the samples from 5 - 95°C in a nondestructive temperature-controlled thermal scanning rigidity monitor (TSRM). A measurable increase in G and decrease in energy damping were observed at lower temperatures for OEW than for EW. In SEW the measurable rheological transitions occurred at the highest temperature ranges. Failure strength of the cooked products (gels) evaluated using torsion and uniaxial compression tests revealed large differences due to treatments. Micrographs of gels showed apparent structural differences among treatments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1984.tb14964.x
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  • 3
    Electronic Resource
    Electronic Resource
    Thermal Denaturation and Aggregation of Actomyosin from Atlantic Croaker (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 47 (1982), 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 denaturation of croaker actomyosin was studied with respect to the important role of coagulation and gelation phenomena in the manufacture of gel-type meat and fish products. Measurements of turbidity (A600), viscosity, calcium ATPase activity, total sulfhydryl groups and protein coagulation of croaker actomyosin solutions during heating at a constant temperature increase of 1°C/min revealed no loss of enzymic activity nor evidence of protein aggregation prior to reaching a temperature of 37–40°C, at which point the protein coagulated with corresponding loss of ATPase activity and sulfhydryl groups and an increase in turbidity. The degree of protein coagulation was highly dependent on the protein concentration. An observed increase in the apparent viscosity over the 30–35°C temperature range was postulated to result from interaction of protein molecules due to noncovalent forces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb12913.x
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  • 4
    Electronic Resource
    Electronic Resource
    Effects of Alkaline Protease in Minced Fish on Texture of Heat-Processed Gels (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), 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: Measurements of properties relating to the physical integrity of heat-processed fish gels varied among samples obtained over a 1-yr period or subjected to various processing temperatures. Such gel properties correlated well with the heat-stable protease (alkaline protease) activity measured in the raw samples. A significant inhibitor concentration-dependent relationship was noted between the addition of a potato derived protease inhibitor and gel strength. These observations support the causative role of an erzymic proteolytic agent in the weakening of gel integrity at processing temperatures near 60°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb04451.x
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  • 5
    Electronic Resource
    Electronic Resource
    Contribution of Retained Organ Tissues to the Alkaline Protease Content of Mechanically Separated Atlantic Croaker (Micropogon undulatus) (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), 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 greater texture breakdown observed in gel-type products prepared from mechanically separated tissue as opposed to manually separated tissue can to some extent be attributed to the significantly higher protease activity measured in mechanically separated tissue. Failure to thoroughly wash eviscerated fish prior to mincing appears to result in the retention of tissue from internal organs as evidenced by a concommitant increase in protease activity in the minced tissue. Alkaline protease activity in croaker kidney and liver is several thousand fold higher than in skeletal muscle. Addition of kidney and liver tissue to deboned tissue from thoroughly washed fish results in increased protease activity and degradation of the fish tissue upon comminuting and cooking at 60°C. Isoelectric focusing provided evidence that the increased alkaline protease activity observed in mechanically separated fish tissue resulted to some degree from retention of kidney tissue in the fish mince. Isolation of Ca++-dependent protease fractions from liver also implicated contamination from this source as an additional contribution to the total protease activity of minced fish.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb04453.x
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  • 6
    Electronic Resource
    Electronic Resource
    Thermal Transitions of Actomyosin and Surimi Prepared from Atlantic Croaker as Studied by Differential Scanning Calorimetry (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: Differential scanning calorimetry (DSC) was used to investigate thermal transitions of fish mince (surimi) and actomyosin from croaker. Three endothermic peaks were observed in DSC thermograms of surimi. After addition of salt, transition temperatures shifted to lower temperatures. Preheating samples containing 3% salt at various temperatures showed that 40°C heating caused the first peak to disappear, and preheating at temperatures higher than 50°C caused virtual disappearance of all transition peaks. Low temperature storage (4°C) of samples caused no significant change in thermograms of salted or unsalted surimi over a 5-day storage period. Evidence suggests that changes of fish protein during low temperature “setting” are different from those occurring during high temperature “setting.”
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13266.x
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  • 7
    Electronic Resource
    Electronic Resource
    Rigidity and Viscosity Changes of Croaker Actomyosin During Thermal Gelation (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: Two types of thermal scanning rigidity monitors (TSRM) were developed which are nondestructive and capable of monitoring rigidity or viscosity changes during heating of proteins over a wide range of concentrations. Thermal transitions which occur during gelation of croaker actomyosin were studied by these TSRM devices and the Brookfield viscometer during constant rate heating (1°C/min). Gelation of actomyosin occurred only at protein concentrations above 5.5% under these conditions. In plots of rigidity versus temperature, three transitions were observed during gelation, occurring near 38°C 46°C and 60°C. At lower concentrations, only one peak was observed, occurring near 36°C. A relationship between the 36–38°C transition in rheological properties and the high temperature “setting” phenomenon of fish proteins is postulated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13267.x
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  • 8
    Electronic Resource
    Electronic Resource
    Thermal Transitions of Admixed Starch/Fish Protein Systems During Heating (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 thermal transitions of starch-fish protein mixtures were investigated by a thermal scanning rigidity monitor technique and differential scanning calorimetry. Three transitions due to protein denaturation and one transition due to starch gelatinization were identified by both techniques during thermal processing of these mixtures. The gelatinization of starch caused an increase in rigidity of the system to a degree dependent upon the starch type. Thermal transitions of starch and fish protein seemed to proceed independently in mixture systems. However, the presence of salt and sucrose, necessitated by the inclusion of fish protein, caused starch gelatinization to shift to higher temperatures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13268.x
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  • 9
    Electronic Resource
    Electronic Resource
    Gel Strength Development During Heating of Surimi in Combination with Egg White or Whey Protein Concentrate (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: Gel strengths (work of penetration) of surimi (refined minced fish, MF) alone and in combination with egg white or whey protein concentrate were periodically measured by an annular pump during constant rate heating. Combination gels containing low percentages of MF were of a lesser strength than an additive relationship would have predicted. However, the strength of gels containing greater percentages of MF did relate to the gel strengths of the uncombined proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb10541.x
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  • 10
    Electronic Resource
    Electronic Resource
    Evaluation of Volume and Pressure Changes During Heating as Indices of Protein Gelation in Fish Pastes (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), 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: A water jacketed piston device was used to monitor pressure and volume changes during heating of lean fish batters. Contrary to published results of a similar study with pork sausage batters, no correlation could be established between thermal gelation phenomena and pressure changes at constant volume. Pressure change at constant volume was nearly linear with respect to temperature change and therefore attributed solely to thermal expansion of the material.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb05059.x
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