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• W2076195770 abstract "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." @default.
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• W2076195770 date "1991-01-01" @default.
• W2076195770 modified "2023-10-16" @default.
• W2076195770 title "Modification of the low-molecular weight basic albumin fraction from rapeseed (Brassica napus L.) by acetylation. Part 2. Selected functional properties" @default.
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• W2076195770 doi "https://doi.org/10.1002/food.19910350306" @default.
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