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  • Articles  (5)
  • Blackwell Publishing Ltd  (5)
  • American Physical Society
  • Cambridge University Press
  • Springer Nature
  • 1990-1994  (5)
  • 1985-1989
  • 1993  (5)
  • Process Engineering, Biotechnology, Nutrition Technology  (5)
Collection
  • Articles  (5)
Source
Publisher
Years
  • 1990-1994  (5)
  • 1985-1989
Year
Topic
  • 1
    Electronic Resource
    Electronic Resource
    EVALUATION OF NUTRITIONAL QUALITY AND FOOD SAFETY OF SEAWEEDS OF INDIA (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food safety 13 (1993), S. 0 
    Details
    ISSN: 1745-4565
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Indian seaweed species Enteromorpha linza, Enteromorpha prolifera, Ulva fasciata, Caulerpa taxifolia and Sargassum johnstonii from natural and cultivated populations were evaluated for food safety and nutritional quality. Among the above seaweeds, Enteromorpha prolifera showed the highest caloric value and protein content, while these values were lowest in Sargassum johnstonii species of natural habitat. The lipid content was maximum in cultivated seaweeds of E. linza and U. fasciata species. Crude fiber varied within a narrow range in all the seaweeds analyzed. Protein efficiency ratio (PER) studies conducted with E. linza and U. fasciata showed low PER values compared to control rats fed on casein as source of protein. Acute oral feeding of seaweeds E. linza, U. fasciata, C. taxifolia and S. johnstonii and subacute oral feeding of E. linza for 12 weeks did not produce any toxic effects on male and female rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4565.1993.tb00096.x
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  • 2
    Electronic Resource
    Electronic Resource
    Dynamic Rheological Measurement of Structure Development in High-methoxyl Pectin/Fructose Gels (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 58 (1993), 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: Incipient structure development (SD) in 65% fructose—0.5, 0.75, and 1% high—methoxyl (HM) pectin gels (pH 2.7) being cooled (50–10°C) were measured in terms of dynamic viscosity (η*) at 1Hz. SD rates (poise/min) were higher at lower temperatures, higher pectin concentrations, and when pectin was hydrated for 16 hr. Below the gel temperature, SD rates in 1% gel followed the Flory-Weaver model. SD in stored 0.5% gels during 22 days was strongly affected by storage temperature (2–38°C) and pH. SD rates in pH 2.7 gels were positive above, but negative below 18°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1993.tb09381.x
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  • 3
    Electronic Resource
    Electronic Resource
    Rheological Properties of Mozzarella Cheese Filled with Dairy, Egg, Soy Proteins, and Gelatin (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 58 (1993), 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 Rheological behavior of mozzarella cheese filled with various proteins (whey protein, caseinate, egg white, soy protein isolate, gelatin) incorporated was determined by uniaxial compression at 10°C and the effect of temperature (10°C−60°C) by dynamic measurement. Mozzarella cheese with whey protein, caseinate, egg white, and soy protein isolate showed significant water retention during heating. Among the proteins, soy protein isolate induced the strongest gel network structure with mozzarella cheese. All proteins altered the viscoelastic properties of mozzarella cheese.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1993.tb06098.x
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  • 4
    Electronic Resource
    Electronic Resource
    Rheological Changes During Gelation of High-Methoxyl Pectin/Fructose Dispersions: Effect of Temperature and Aging (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 58 (1993), 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: Gels made with 0.5% and 1% pectin in 60% fructose, and a commercial sample exhibited macromolecular solution/weak gel behavior. Cooling the gels from 50–10°C increased storage (G') and loss moduli (G') of the gels. As the rate of cooling (10, 5.7, and 2.5°C/hr) a 1% pectin, 60% fructose, dispersion increased, the elasticity of the formed gel decreased; however, G' was not affected much by rate of cooling. During the first 24 hr, the changes in G'and G' were small. After 14 days storage at ambient temperature, G’values of gels increased substantially, while G' values increased slightly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1993.tb03237.x
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  • 5
    Electronic Resource
    Electronic Resource
    Gel Point of Whey and Egg Proteins Using Dynamic Rheological Data (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 58 (1993), 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 gel point temperatures of coagulation type proteins and gelation type proteins were determined by extrapolating the rapidly rising phase of the storage modulus G’back to the temperature axis. The gelation onset. temperatures of the concentration-independent proteins oval-bumin, ovotransferrin, and BSA were 81°C, 62°C, and 75°, respectively, Gelation of whey protein isolate and egg white gels, both concentration-dependent, was presumably due to disulfide bonds formed by the interactions of the concentration-independent proteins: α-lac-talbumin and β-lactoglobulin, and ovalbumin and ovotransferrin, respectively. Moreover, the incipient gel temperature of whey proteins decreased when the concentration of whey proteins increased.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1993.tb03223.x
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