Abstract
Egg white proteins are an excellent source of nutrition, with high biological and technological values. However, their limited functional properties prevent their widespread industrial applications. In this study, the ovalbumin functionality was improved via glycation by Maillard reaction with d-lactose. The free amino groups and sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile were determined, confirming that glycation occurred between ovalbumin and lactose. The emulsification of the conjugate was 2.69-fold higher than that of ovalbumin at pH 7.0 after glycation. The thermal stability also improved remarkably. The glycated protein products were used to form an oil-water nanoemulsion for polymethoxyflavone-rich aged orange peel oil. The resulting nanoemulsion showed good pH, thermal, and storage stabilities.
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