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1990•Journal of the Science of Food and AgricultureRequires access

Effect of succinylation on the functional and physicochemical properties of bovine serum albumin

Margaret C. Murphy, Nazlin K. Howell

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Abstract

Abstract Bovine serum albumin was modijed with succinic anhydride so that 50 or 82% of lysine residues were acylated. The structural alterations caused by modification were examined by pH titration, electrophoretic patterns, circular dichroism, amino acid analysis, and the measurement of amino, sulphydryl and hydrophobic groups. Changes in these physicochemical properties were related to inferior whipping, emulsification and gelling properties of succinylated bovine serum albumin compared with the native protein.

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What this paper is about

Abstract Bovine serum albumin was modijed with succinic anhydride so that 50 or 82% of lysine residues were acylated. The structural alterations caused by modification were examined by pH titration, electrophoretic patterns, circular dichroism, amino acid analysis, and the measurement of amino, sulphydryl and hydrophobic groups. Changes in these physicochemical properties were related to inferior whipping, emulsification and gelling properties of succinylated bovine serum albumin compared with the native protein.

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Available abstract

Abstract Bovine serum albumin was modijed with succinic anhydride so that 50 or 82% of lysine residues were acylated. The structural alterations caused by modification were examined by pH titration, electrophoretic patterns, circular dichroism, amino acid analysis, and the measurement of amino, sulphydryl and hydrophobic groups. Changes in these physicochemical properties were related to inferior whipping, emulsification and gelling properties of succinylated bovine serum albumin compared with the native protein.

Key concepts: Succinylation, Succinic anhydride, Bovine serum albumin, Chemistry, Lysine, Titration, Circular dichroism, Serum albumin

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