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  • 1
    Electronic Resource
    Electronic Resource
    New Photosynthesis: Direct Photoconversion of Biomass to Molecular Oxygen and Volatile Hydrocarbons (1995)
    s.l. : American Chemical Society
    Energy & fuels 9 (1995), S. 163-167 
    Details
    ISSN: 1520-5029
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ef00049a024
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  • 2
    Electronic Resource
    Electronic Resource
    Production of Nonbitter, Desalted Milk Hydrolysate for Fortification of Soft Drinks and Fruit Juices (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 simpler and less expensive process than the process of Helbig et al. (1980) for preparation of a nonbitter, desalted milk hydrolysate is presented. Skim milk was hydrolyzed with Alcalase (subtilisin Carlsberg) at 50°C in 3 hr. The resin in OH form was added to milk batchwise to simultaneously raise the pH to 8.5 for optimum proteolysis and exchange the anions in milk which contributed to saltiness. These modifications resulted in a shorter hydrolysis time and a more economical resin regeneration than those of the Helbig process. The dried milk hydrolysate was added to soft drinks and fruit juices at solids concentrations up to 10% (3% protein) without adverse effects on their taste, color, viscosity and clarity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb14925.x
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  • 3
    Electronic Resource
    Electronic Resource
    Studies of Thermal Denaturation of Oat Globulin by Differential Scanning Calorimetry (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), 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: Thermal denaturation of oat globulin was studied by differential scanning calorimetry (DSC). Prior heat treatments at 100°C and 110°C resulted in a progressive decrease in enthalpy (ΔH) indicating partial denaturation. Marked increase in denaturation temperature (Td) and onset temperature (Tm) and decrease in width at half peak height (ΔT1/2) suggest that the preheated protein assumed a more compact conformation or associated to a complex structure with higher thermal stability and cooperativity. The heated globulin was segregated into soluble and insoluble fractions containing native and denatured protein respectively. The denaturation kinetics of oat globulin was studied and results show a reaction order of 2.5 and an activation energy of 505 KJ/mol. Heat treatments caused a pronounced increase in activation energy and pre-exponential factor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1988.tb07749.x
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  • 4
    Electronic Resource
    Electronic Resource
    Study of Thermal Properties of Oat Globulin by Differential Scanning Calorimetry (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), 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 behavior of oat globulin was studied by differential scanning calorimetry (DSC). The effects of pH, salts, and of various structure perturbants upon thermal characteristics were determined. Raising or lowering pH from near neutrality reduced denaturation temperature. (Td), enthalpy (ΔH) and cooperativity indicated by increase in width at half height (ΔT1/2). The effect of salts on thermal stability was related to their position in the lyotrophic series and suggests involvement of hydrophobic interaction in the thermal stability of oat globulin. Increasing concentrations of urea progressively lowered Td and ΔH and increased ΔT1/2; sodium dodecyl sulfate (SDS) lowered ΔH without affecting Td; ethylene glycol (EC) lowered Td without changing ΔH. Dithiothreitol did not affect DSC characteristics suggesting that disulfide bonds do not contribute to the thermal response of oat globulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb06622.x
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  • 5
    Electronic Resource
    Electronic Resource
    Rheological and Structural Properties of Egg White/Oat Globulin Co-Gels (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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: Co-gels of egg white (EW) and oat globulin (native and deamidated) were prepared by heating mixtures of the two proteins at different ratios. Rheological properties of the co-gels were assessed by small amplitude oscillatory tests. Storage (G′) and loss (G″) moduli of the co-gels increased with increases in EW content in the mixtures. At comparable EW/non-EW ratios, EW formed much stronger co-gels with deamidated oat globulin (DOG) than with native globulin (OG) or several other non-EW proteins. Microscopic examination of mixed gels revealed structural differences between EW/OG and EW/DOG co-gels. The former exhibited a two gel system with OG distributed discontinuously throughout the supporting EW matrix. DOG and EW formed a homogenous gel network, demonstrating compatibility between the two proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb06026.x
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  • 6
    Electronic Resource
    Electronic Resource
    Elimination of β-Lactoglobulin from Whey to Simulate Human Milk Protein (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: When the pH of cottage cheese whey was adjusted to 4.5 in the presence of 6.7 mM FeCI3, β-lactoglobulin was eliminated from the whey as a precipitate. However, the majority of immunoglobuhns were also coprecipitated. To recover immunoglobulins together with α-lactalbumin, the whey pH was adjusted to 3.0 in the presence of 4.0 mM FeCI3. After centrifugation of the whey, the supernatant contained exclusively β-lactoglobulin; other whey proteins were found in the precipitate. Excess Fe+++ in the precipitate was removed by ion exchange or by ultrafiltration. This protein concentrate had a protein composition much more similar to that of human milk whey than that of ultrafiltered whey protein concentrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13755.x
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  • 7
    Electronic Resource
    Electronic Resource
    Study of Acetylated Food Proteins by Raman Spectroscopy (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: : Three food proteins, soy protein isolates, spray-dried egg white, and whey protein isolates, were acetylated to varying levels, and the extent of modification was determined by wet chemistry methods. Raman spectra of the modified proteins were obtained. A new C=O stretching vibration was observed at 1737cm-1 and was attributed to ester carbonyl groups appended to the proteins during acetylation. Calibration curves were obtained by plotting the intensity ratio of this Raman band to the 1003cm-1 phenylalanine stretching band against the extent of substituted hydroxyl groups. Linear fits were obtained with correlation coefficient r〉 0.9979. The Raman spectral data were also analyzed to study the effect of acetylation on the conformation of the 3 proteins. Marked conformational changes were observed in the modified proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2004.tb13359.x
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  • 8
    Electronic Resource
    Electronic Resource
    Modification of Proteins from Soymilk Residue (Okara) by Trypsin (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: Okara protein isolates were hydrolyzed by trypsin to about 5% to 14%. Solubility was increased more than twofold by the modification, and water hydration capacity and emulsification activity index were also improved. The okara protein products had good essential amino acid profiles and the trypsin-hydrolysates also had increased in vitro digestibility and available lysine content. The low solubility of okara protein makes it difficult to incorporate it into many food systems. Okara protein hydrolysates, with improved solubility and other functional properties, could be used as a low-cost protein ingredient in processed foods.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb15911.x
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  • 9
    Electronic Resource
    Electronic Resource
    Standardized Failure Compression Test of Protein Gels from a Collaborative Study (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 62 (1997), 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 failure compression test with a standardized procedure for protein gelation was developed. Using whey protein concentrate, egg white protein and soy protein isolate as representative proteins, a highly reproducible procedure for sample preparation and gel testing was developed after refinements. Gels of varying protein concentrations were prepared with 0.1 M NaCl at pH 7. Force (N) and strain (Δh/h) at failure were the main parameters measured. Variability of results was found due to uncontrolled conditions for protein hydration and pH adjustment and air incorporation during hydration. After corrective steps to avoid potential errors, the procedure was recommended for a routine analysis of failure properties of protein gels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1997.tb12236.x
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular weight distribution of interacting proteins calculated by multiple regression analysis from sedimentation equilibrium data: An interpretation of α"s"1-κ-casein interaction
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 195 (1979), S. 596-606 
    Details
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-9861(79)90386-2
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