Abstract
ABSTRACTThe ovalbumin denaturation induced by Maillard reaction with glucose was investigated by immunochemical methods. The storage for either 2 or 10 days at 50°C and 65% relative humidity decreased the maximum immunoprecipitation to 90 and 80% of that by native protein, respectively. Ten day‐stored ovalbumin was separated into two fractions with antigenicity (fr‐II) and without (fr‐I) by the immunoaffinity chromatography of antiovalbumin‐coupled Sepharose 4B. The circular dichroism (CD) analysis showed that fr‐II, containing amino groups in almost the same amount as fr‐I, retained a large amount of ordered structure. Ovalbumin molecules were presumably not denatured by only the modification of amino groups with glucose in an early stage of Maillard reaction.
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