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  • Articles  (3)
  • Articles: DFG German National Licenses  (3)
  • Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition  (3)
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  • Articles  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Ultraviolet Radiation Affects Physical and Molecular Properties of Soy Protein Films (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 63 (1998), 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: Films were cast from heated, alkaline aqueous solutions of soy protein (5 g/100 mL water) and glycerin (50% w/w of protein). Control and ultraviolet (UV) irradiated (13.0, 25.9,38.9, 51.8, 77.8, or 103.7 J/m2) films were evaluated for tensile strength (TS), elongation at break (E), water vapor permeability (WVP), and Hunter L, a, and b color values. TS increased (p〈0.05) linearly while E decreased linearly with UV dosage. WVP was not affected (P〉0.05) by UV irradiation. UV treatment intensified the yellowish coloration of films (increased +b values). SDS-PAGE patterns for UV-treated samples revealed bands of aggregates, increasing in intensity with UV dosage, which were absent in control samples. These changes suggested UV-induced cross-linking in films.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1998.tb15714.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Tensile, Solubility, and Electrophoretic Properties of Egg White Films as Affected by Surface Sulfhydryl Groups (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: Films plasticized with polyethylene glycol were cast from alkaline (pH 10.5, 11.0, or 11.5), aqueous egg white (EW) solutions with or without heating (40°C for 30 min). Prior to casting, concentration of surface sulfhydryl (SH) groups was determined and they increased (P 〈 0.05) (3.81–19.45 μM/g protein) with both pH and heating, presumably due to protein denaturation and cleavage of disulfide (S-S) bonds. Concentration of surface SH groups correlated (P 〈 0.05) with film tensile strength (r = 0.70), elongation at break (r = 0.86), and film total soluble matter (r =−0.94). Most likely, surface SH groups formed S-S bonds through air oxidation and/or sulfhydryl/disulfide interchange, thus contributing to EW film formation. SDS-PAGE patterns in presence or absence of 2-mercaptoethanol confirmed occurrence of S-S bonding in dried EW films.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb09865.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Physical and Molecular Properties of Egg-white Lipid Films (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: Polyethylene glycol-plasticized films were cast from alkaline (pH 11.25), heated (45 °C for 20 min), aqueous egg white (EW) solutions, with or without (10% or 20% w/w of EW) milkfat (two fractions), oleic acid, or egg yolk lysophospho-lipid (LPL). The lipids did not reduce (P 〉 0.05) film water vapor permeability. Oleic acid increased (P 〈 0.05) tensile strength and elongation, and surface sulfhydryl group (SH) concentrations in EW solutions. Oleic acid probably increased negative charges on EW proteins, unfolding protein chains, and exposing SH groups. LPL also slightly increased (P 〈 0.05) surface SH concentrations in non-heated mixtures. Electrophoretic patterns suggested oleic acid interactions with ovalbumin, ovotransferrin, and lysozyme. No lysinoalanine was in film-forming mixtures based on lysine measurements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb15928.x
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    Paper (German National Licenses)
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