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7735945 
Journal Article 
Chemical composition, functional properties, and bioactivities of rapeseed protein isolates 
Yoshie-Stark, Y; Wada, Y; Waesche, A 
2008 
Yes 
Food Chemistry
ISSN: 0308-8146
EISSN: 1873-7072 
ELSEVIER SCI LTD 
OXFORD 
107 
1 
32-39 
English 
WOS:000251535800005 
In order to utilize rapeseed protein from oil industry waste for food applications, rapeseeds were pretreated to remove the oil using hexane. Two protein isolates were prepared, one by precipitation at controlled pH and the other by ultrafiltration. The precipitated and ultrafiltered protein isolates, respectively, contained 70.8% and 98.7% protein. The ultrafiltered protein isolate had a better emulsification capacity than had whole egg. The ultrafiltered protein isolate had a protein solubility of 52.5-97.2% in the range pH 3-9, whilst the maximum protein solubility of the precipitated protein isolate was 26.4% in the pH range 7-9. There were no significant differences between the precipitated and ultrafiltered protein isolates regarding their angiotensin converting enzyme inhibition are their bile acid-binding capacity. Their bile acid-binding capacity and angiotensin converting enzyme inhibition capacities were lower than of those de-oiled soybean. They showed stronger DPPH radical-scavenging activity than did de-oiled soybean. © 2007 Elsevier Ltd. All rights reserved. 
Brassica napus; protein isolate; functional properties; ACE inhibition; bile acid-binding; DPPH radical-scavenging activity