Ovalbumin: A potential functional protein

Although ovalbumin makes up 54% of the total egg white proteins, individual protein usage is rare. The primary applications of ovalbumin in the food industry relate to other proteins, such as whole egg whites. Ovalbumin has remarkable functional properties, such as those of gelation, foaming, and em...

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Bibliographic Details
Published inFood Science and Preservation Vol. 31; no. 3; pp. 346 - 359
Main Authors Udeshika Maggonage, Maggonage Hasini, Manjula, Prabudhdha, Ahn, Dong Uk, Nalaka Sandun Abeyrathne, Edirisingha Dewage
Format Journal Article
LanguageEnglish
Published 한국식품저장유통학회 01.06.2024
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Summary:Although ovalbumin makes up 54% of the total egg white proteins, individual protein usage is rare. The primary applications of ovalbumin in the food industry relate to other proteins, such as whole egg whites. Ovalbumin has remarkable functional properties, such as those of gelation, foaming, and emulsification, which are crucial in the processing of food, however, its application as a standalone functional protein is severely constrained due to separation issues. In recent years, new methodologies for the large-scale separation of ovalbumin have emerged. Meantime, ovalbumin was identified as a good source to produce bioactive peptides with a variety of functional properties, including antibacterial, antioxidant, and angiotensin-converting-enzyme inhibitory actions, according to research. Newly discovered bioactive peptides from ovalbumin can be used in the food sector in addition to their well-known functional properties to create health-promoting products. Benefits extend beyond the food business to numerous other sectors, such as the pharmaceutical and cosmetic industries. Consequently, a gap between the existing and prospective future uses is found. The main goals of this study were to determine some possible factors for the long-term neglect of the major protein and to determine the growing potential for applications of ovalbumin and peptides.
ISSN:3022-5477
3022-5485
DOI:10.11002/fsp.2024.31.3.346