Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Protein and carbohydrate fractions in oat flour were separated on the basis of density using nonaqueous solvent systems. Optimum solvent densities and solvent:flour ratios for maximum yield of protein fraction were determined. Fractions with over 70% protein content can be separated; however, they represent only about 40% of the protein available in the flour. The carbohydrate fraction contains about 10% protein, with approximately half the protein available in the flour remaining in this fraction. Functional properties of the protein fractions such as hydration capacity, emulsifying activity, emulsion stability and nitrogen solubilities were determined.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Up to 4% oat protein concentrates can fortify either neutral or acidic beverages. The concentrate was produced in good yield from both defatted and non-defatted oat groats by alkaline extraction. If desired, the gum and water-soluble protein fractions can be removed by a preliminary water extraction yielding a concentrate with a higher percentage of protein. Nitrogen solubility of protein concentrate from defatted groats in dilute phosphoric acid was considerably higher than one from nondefatted groats. Fortified acidic beverages (pH 3) prepared with oat concentrate from laboratory ground groats were slightly astringent in taste. However, astringency was eliminated if the concentrate was produced from commercial oat flour (heat treated during production). Milklike and breakfast-type beverages fortified with oat protein concentrate would be nutritious, palatable and easily prepared and flavored.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 42 (1991), S. 1701-1709 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Chiroptical methods have been used to study the conformation and interactions of amylose and amylopectin with poly(ethylene co-acrylic acid) (EAA) in aqueous solution. These studies, along with X-ray diffraction and solid-state NMR data, show that amylose and EAA, as well as amylopectin and EAA, form helical V-type inclusion complexes when mixed in aqueous suspension. This structure apparently accounts for the partial compatibility observed in films containing starch and EAA. About 2/3 by weight of EAA does not interact with amylose and probably represents the ethylene-rich central core of the EAA micelle. EAA/amylose complexes in 10 mM NaOH were stable to temperatures 〉 90°C, whereas EAA/amylopectin complexes in the same solvent were largely disrupted at this temperature. Urea, at a concentration of 8 M, further destabilized both EAA/amylopectin and EAA/amylose complexes. Solutions with an alkaline pH (〉 9.5) dispersed EAA optimally and allowed maximum complexing with amylose. At pH values 〉 13, the EAA/amylose complexes were weaker, most likely due to electrostatic repulsion between ionized hydroxyl groups of amylose and carboxyl groups of EAA.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...