Functional properties of plant proteins. Part 8. Effect of succinylation on some functional properties of the main globulin fraction from rapeseed (Brassica napus L.)

✍ Scribed by Nitecka, Elzbieta ;Schwenke, K. D.

• Publisher: John Wiley and Sons
• Year: 1986
• Tongue: English
• Weight: 348 KB
• Volume: 30
• Category: Article
• ISSN: 0027-769X
• DOI: 10.1002/food.19860301002

✦ Synopsis

The changes of some functional propertiessolubility, emulsifying and foaming properties, heat-induced aggregationof a native rapeseed globulin preparation after succinylation has been studied. In correspondence with the results obtained with the purified rapeseed 12 S globulin and other globulin preparations from plant seeds, a total blocking of the amino groups of the rapeseed globulin could not be attained. The highest degree of modification reached was 837;. The unmodified protein has high foam capacity and stability. Succinylation until 61 7; did not change these properties. The emulsifying activity and emulsion stability were slightly improved after a modification at a low or moderate level. The heat-coagulation of the native protein is depressed by increasing succinylation.