Modification of the low-molecular weight basic albumin fraction from rapeseed (Brassica napus L.) by acetylation. Part 2. Selected functional properties

✍ Scribed by Schwenke, K. D. ;Kim, Y. H. ;Kroll, J. ;Lange, Erika ;Mieth, G.

• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: English
• Weight: 451 KB
• Volume: 35
• Category: Article
• ISSN: 0027-769X
• DOI: 10.1002/food.19910350306

✦ Synopsis

The influence of acylation on surface functional properties, solubility and heat-induced aggregation of the low-molecular weight basic protein fraction (napin) from rapeseed was studied. While the native protein was soluble over the whole pH-range, the exhaustively acetylated one became precipitable in the weakly acidic range. Acetylation of 70-80% of the protein amino groups caused a stabilizing against heat-induced aggregation. The native protein had a high foam capacity and stability which were only slightly changed after acylation. Decreasing volume specific work in the order native>acetylated > succinylated protein pointed, however, to an improved foamability of acylated napin. Succinylation increased the interfacial tension on the oil/water interface, while acetylation gave both an increasing and a decreasing effect depending on the degree of modification. The emulsifiying capacity decreased after acylation in the order native > acetylated > succinylated.