New processing of lupin protein isolates and functional properties.
A growing demand for functional plant proteins could be identified, which properties are customized for specific applications and formulations as food ingredients. Native lupin proteins (alpha, beta, gamma) conglutin have a good solubility at appropriately chosen conditions. A novel procedure has been proposed to maintain the native protein properties. Lupin proteins are extracted from hexane deoiled lupin. The protein product type E comprises high molecular weight proteins (alpha, beta-conglutin), which are separated using alkaline extraction and acid precipitation procedures. The protein product type F is enriched in the gamma-conglutin fraction and is separated from the acid pre-extract applying cross flow filtration at pH 7-8. For the zirconium oxide membrane the filtration rate can be increased by appropriately chosen pH conditions up to 70 l/m2h. Lupin protein fraction (type E and F) are highly soluble protein isolates with outstanding emulsification, salt tolerance and foaming properties. These new lupin proteins (type E and F) offer extremely interesting properties for application in food systems and are available from pilot plant fractionation.
Wäsche
A
A
Fraunhofer-Institute for Process Engineering and Packaging, Department of Process Engineering, Giggenhauserstrasse 35, D-85354 Freising, Germany. wae@ivv.fhg.de
Müller
K
K
Knauf
U
U
D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000737:chemistry* / Q000502:physiology; D005524:Food Technology; D006863:Hydrogen-Ion Concentration; D014674:Plant Proteins, Dietary / Q000737:chemistry* / Q000378:metabolism*; D012639:Seeds / Q000737:chemistry* / Q000502:physiology; D012995:Solubility
D014674:Plant Proteins, Dietary