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Property Profiles of Isolated Plant Proteins for Assessing their Potential for Processing and Application

 
: Müller, K.; Wäsche, A.; Borcherding, A.

Santen, E. van ; International Lupin Association:
Lupin - An Ancient Crop for the New Millenium. Proceedings of the 9th International Lupin Conference. Klink/Müritz, Germany 20-24 June 1999
Canterbury, New Zealand: International Lupin Association, 2000
ISBN: 0-86476-123-6
S.461-463
International Lupin Conference <9, 1999, Klink/Müritz>
Englisch
Konferenzbeitrag
Fraunhofer IVV ()
isolated protein; water binding; process parameter; property profile

Abstract
The effects of process parameters on the water binding capacity of isolated proteins from lupins (L. albus cv. Amiga) have been studied. The results show that the water binding capacity can be tailored in the range from 2 to about 5 g g-1 by process control. Native proteins from lupins are characterized by their high resolvability in water (about 65-85 g 100 g-1) and low water binding capacity (< 2 g g-1). A comparison of the property profiles of commercial isolated proteins from various sources having similar resolvability and similar water binding capacity indicates that other product properties such as emulsifying capacity and oil binding capacity can show large differences. The purposeful selection of a custom-designed protein for a specific application is made easier by using comprehensive property profiles. This is useful because the resolvability and interfacial properties critically affect the quality features of the finished food product, such as the texture, viscosity and stability in the complex systems in which proteins are used.

: http://publica.fraunhofer.de/dokumente/N-3950.html