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  • 1
    Electronic Resource
    Electronic Resource
    Role of calcium in activating soybeam lipoxygenase 2 (1974)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 22 (1974), S. 802-805 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60195a006
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  • 2
    Electronic Resource
    Electronic Resource
    Cooxidation of .beta.-carotene by an isoenzyme of soybean lipoxygenase (1977)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 25 (1977), S. 124-127 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60209a046
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Measurement of unfrozen and free water in soy proteins by differential scanning calorimetry (1980)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 28 (1980), S. 1303-1305 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60232a069
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  • 4
    Electronic Resource
    Electronic Resource
    The Autoxidation of Crystallized Beef Myoglobin (1961)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 26 (1961), 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 autoxidation rate in air for crystallized beef muscle myoglobin and the temperature dependence of the autoxidation were studied. Results show that autoxidation of beef muscle myoglobin is essentially the same as that reported by others for horse heart myoglobin. The rate constant for autoxidation was found to be dependent upon the amount of sodium hydrosulfite used to reduce metmyoglobin. It was shown that increased autoxidation, resulting from relatively high concentrations of sodium hydrosulfite, was not due to hydrogen peroxide. Control of the amount of sodium hydrosulfite used to 0.005% or less substantially reduced fluctuations observed in rate constants for autoxidation. For crystallized beef muscle myoglobin at pH 5.7 and 30°C, the rate constant is 0.21 ± 0.02 hr−1. The abnormally high temperature dependence of myoglobin autoxidation and the relative importance of bacteria and autoxidation as causes of meat discoloration were discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1961.tb00391.x
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  • 5
    Electronic Resource
    Electronic Resource
    EVALUATION OF HEATED SOY FLOURS BY MEASUREMENT OF TRYPTIC HYDROLYSIS USING A pH STAT (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 45 (1980), 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: This is an exploratory account of the feasibility of using a pH stat to measure tryptic hydrolysis of soy flours that had been heated to different extents. Initial rates of hydrolysis could be determined in 1 to 2 min, and by measuring proteolysis rates at several trypsin amounts, useful information about residual trypsin inhibitor and about heat denaturation of the soy protein could be obtained. There were variations in rates due to substrate concentrations and due to instrumental parameters that need to be understood to take full advantage of this method.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb07482.x
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  • 6
    Electronic Resource
    Electronic Resource
    Measurement of Discoloration in Fresh Beef (1964)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 29 (1964), 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 method is described whereby precise measurement of discoloration in fresh red meats can be achieved. The method utilizes α values obtained from Gardner automatic color-difference meter readings and depends upon careful control of storage temperature, control of sample area from which readings are taken, and consistent orientation of sample during subsequent readings.Results obtained with the method indicate considerable variation in discoloration of samples from the same slice of beef round stored at 6°C; a substantial decrease in discoloration with lowered storage temperature; a decrease in discoloration resulting from increased exposure of the sample to air; and the probable importance of respiration by the meat rather than bacterial contamination in determining discoloration at low temperatures (-2°C).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1964.tb00407.x
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  • 7
    Electronic Resource
    Electronic Resource
    Use of the pH Stat to Evaluate Trypsin Inhibitor and Tryptic Proteolysis of Soy Flours (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: Heated soy flours have been analyzed by the pH stat successfully for tryptic proteolysis and for residual trypsin inhibitor in previous studies. Unheated soy flours give a sudden release of hydrogen ion followed by a constantly decreasing proteolysis rate and consequently are difficult to analyze. We have found that by adjusting the pH of the trypsin preparation to 9 (the pH of the analysis) the pH stat method measured proteolysis and trypsin inhibitor in unheated soy flours. The unheated soy protein was hydrolyzed at 40% of the rate of heated soy protein and contained 68 mg/g of Kunitz trypsin inhibitor equivalents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb12935.x
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  • 8
    Electronic Resource
    Electronic Resource
    PRODUCTION AND BINDING OF MALONALDEHYDE DURING STORAGE OF COOKED PORK (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 37 (1972), 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: Cooked pork samples were stored at 3°C and analyzed for malonaldehyde (MA). MA increased to a maximum and remained there, typical behavior for a food but contrasting with pure lipid oxidation in which MA increases and then decreases as volatile MA is lost. The failure to lose MA in food products may be attributed to MA binding. Water extracts of cooked pork samples (representing approximately l /3 of the total MA) were fractionated on G-10 Sephadex and analyzed for MA. With increasing storage time, a definite change in elution pattern from free MA to bound MA took place; the binding was not to protein or amino acids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1972.tb02720.x
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  • 9
    Electronic Resource
    Electronic Resource
    Co-dried Carbohydrates Effect on the Performance of Egg Yolk Solids (1968)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 33 (1968), 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: SUMMARY– When egg yolk is dried and subsequently rehydrated, it loses its ability to form a stable foam. If sufficient carbohydrates are added to the egg yolk before dehydration, much of the foaming ability is retained by the rehydrated yolk. Evidence has been presented that, in plain-dried yolk, the removal of water irreversibly changes the structure of the low-density lipoproteins and that foam-inhibiting free lipid is released from these lipoproteins. When yolk is co-dried with added carbohydrates, the carbohydrates partially protect the lipoproteins from this irreversible structural change, probably by replacing the water of hydration at its binding sites during the drying process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1968.tb03665.x
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