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1987•Journal of the American Oil Chemists SocietyRequires access

Effects of limited proteolysis on functional properties of ovalbumin

Etsushiro Doi, Taihei Koseki, Naofumi Kitabatake

Open publisher page 31 citations

Abstract

Abstract We examined the limited proteolysis of ovalbumin by pepsin and its effect on the functional properties of the ovalbumin. Pepsin hydrolyzed only the single peptide bond of ovalbumin between His‐22 and Ala‐23. This provided a large intermediate (MW 42,500), P‐ovalbumin. A P‐ovalbumin solution gave a transparent gel when heated. Under the same conditions, an ovalbumin solution gave a turbid gel. We studied the physicochemical properties of P‐ovalbumin and the formation of the transparent gel.

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What this paper is about

Abstract We examined the limited proteolysis of ovalbumin by pepsin and its effect on the functional properties of the ovalbumin. Pepsin hydrolyzed only the single peptide bond of ovalbumin between His‐22 and Ala‐23. This provided a large intermediate (MW 42,500), P‐ovalbumin. A P‐ovalbumin solution gave a transparent gel when heated. Under the same conditions, an ovalbumin solution gave a turbid gel. We studied the physicochemical properties of P‐ovalbumin and the formation of the transparent gel.

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Available abstract

Abstract We examined the limited proteolysis of ovalbumin by pepsin and its effect on the functional properties of the ovalbumin. Pepsin hydrolyzed only the single peptide bond of ovalbumin between His‐22 and Ala‐23. This provided a large intermediate (MW 42,500), P‐ovalbumin. A P‐ovalbumin solution gave a transparent gel when heated. Under the same conditions, an ovalbumin solution gave a turbid gel. We studied the physicochemical properties of P‐ovalbumin and the formation of the transparent gel.

Key concepts: Ovalbumin, Proteolysis, Pepsin, Chemistry, Hydrolysis, Peptide, Chromatography, Biochemistry

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