Chemical modification of proteins. Part 12. Effect of succinylation on some physico-chemical and functional properties of the albumin fraction from rapeseed (Brassica napus L.)

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

• Publisher: John Wiley and Sons
• Year: 1986
• Tongue: English
• Weight: 606 KB
• Volume: 30
• Category: Article
• ISSN: 0027-769X
• DOI: 10.1002/food.19860301003

✦ Synopsis

The effect of succinylation on native rapeseed albumin was studied using polyacrylamide gel electrophoresis (PAGE), isoelectric focusing, viscometry. turbidimetry and by investigation of some functional properties (heat-induced aggregation. emulsifying and foaming properties). The protein can be quickly modified with a relatively small excess ofsuccinic anhydride. A 98 % succinylation of the protein amino groupscould be attained. The PAGE patterns point out a relatively high heterogeneity of the succinylated protein. The isoelectric focusing shows. however, a concentration of the succinylated protein fractions in a near pl range (pH 4.45 to 4.60). The intrinsic viscosity [q] of the native albumin drops after a 50% succinylation from 0.15 dl . g-' to 0.06-0.07 dl . g Increasing the degree of succinylation to 880, increases [q] to 0.09 dl g -' , The native albumin possesses excellent whipping properties and high foam stability. Succinylation did not improve the foam capacity but decreases the foam stability. The emulsifying properties could not be improved by succinylation. The heat-induced aggregation of the rapeseed albumin in dilute solution is inhibited by a moderate or high succinylation.