OVOTRANSFERRIN: The nutraceutical protein with antimicrobial, antioxidant, and immunomodulatory properties
OVOTRANSFERRIN (also known as CONALBUMIN) is a significant component of the avian egg’s innate antimicrobial defense system1,2, protecting the developing chick from invading pathogens. This property arises primarily through its iron (Fe3+) binding capacity by locking away a critical biochemical component necessary for micro-organismal survival. Bacteria starved of iron are incapable of moving, making OVOTRANSFERRIN a potent bacteriostatic3. OVOTRANSFERRIN is also bactericidal independently of its iron-binding properties; its cationic (positively charged) nature ruptures bacteria by driving attachment directly to the bacterial surface4-6. Antifungal7 and antiviral8 properties have also been identified, making OVOTRANSFERRIN a safe and natural protein with applications across various industries.
It is not only the intact OVOTRANSFERRIN protein that possesses industrially exploitable properties. Hydrolyzed peptides generated by gastrointestinal digestion, food processing, and direct hydrolysis exhibit potent antimicrobial9, anti-hypertensive10-13, anti-osteoporotic14-16, and antioxidant properties17,18. Beyond this, toxicity to cancer cells19 and immunomodulatory20,21 functionalities have also been identified.
Bioseutica® is the largest manufacturer and supplier of OVOTRANSFERRIN globally. Our advanced SOLVENT-FREE extraction and purification processes result in a highly pure, high-quality protein that our customers have relied on since the 1970s.
Functional foods: antimicrobial, edible films, and emulsions
A potent antibacterial possessing both bacteriostatic and bactericidal capabilities, OVOTRANSFERRIN has broad appeal in the food industry. OVOTRANSFERRIN has found effective use as a component of edible protective films, increasing the shelf-life of fresh meats and in Asian cuisine22. OVOTRANSFERRIN may also be an edible, surfactant-free emulsifying component, preventing fat-water separation in foods, including UHT milk, mayonnaise, ice cream, margarine, and batter 23. Its similarity to lactoferrin holds promise for OVOTRANSFERRIN’s use in supplemented infant formula, milk, yogurts, and nutritional supplements.
Feed industries: decrease poultry mortality and antibiotic use
Aerosolized OVOTRANSFERRIN has been used as an antibacterial in large-scale turkey farming, reducing mortality and preventing respiratory disease, decreasing the requirement for antibiotic use24.
Lactoferrin Alternative: food, cosmetic, and oral care
As a member of the transferrin family, OVOTRANSFERRIN is functionally and structurally analogous to mammalian lactoferrin25. A recent study has shown the superior performance of OVOTRANSFERRIN compared to lactoferrin in its ability to deliver iron without accumulation or inducing gastric irritability26.
OVOTRANSFERRIN represents an excellent substitute for lactoferrin, which is widely used in the food, cosmetic, and oral care industries27. Products using its antimicrobial, antioxidant, iron absorption, and hygiene-promoting properties include infant formula, dietary supplements, pet food, lotions, face wash, mouthwash, toothpaste, and chewing gum.
Pharmaceuticals, medical, and wellness industries
Research into OVOTRANSFERRIN's pharmaceutical and medical applications and its derived peptides has revealed exciting potential functions. Studies have identified dual anti-osteoporotic properties of OVOTRANSFERIN, both reducing bone resorption and promoting bone formation14. Beyond this, OVOTRANSFERRIN shows promise as a drug carrier with potential applications in cancer treatment19. Indeed, OVOTRANSFERRIN alone is toxic to cancer cells in-vitro. Its antioxidant17,18 and anti-inflammatory properties may also make OVOTRANSFERRIN a viable treatment for cardiovascular diseases10-13.
Recent work has identified OVOTRANSFERRIN as an excellent potential iron carrier for treating iron deficiency anemias (IDA)26. OVOTRANSFERRIN showed superior physiological iron delivery over lactoferrin in a gastric barrier model. This data holds much promise for OVOTRANSFERRIN’s use in food supplements, with dual functionality as antimicrobial and iron delivery mechanisms.
OVOTRANSFERRIN is a protein that has a high similarity to Bovine lactoferrin (BLF) and human lactoferrin (HLF) and may be used as a substitute for lactoferrin (LF) due to its limited production. While there were differences in isoelectric point, particle size, and hydrophobicity, it was still able to maintain good dispersity with similar denaturation temperatures. OVOTRANSFERRIN is more sensitive to heating at a pH of 5.0. Compared to BLF, OVOTRANSFERRIN had a higher secondary structure stability at pH 7.0 and 9.0. In addition, OVOTRANSFERRIN has a lower thermal aggregation degree than BLF and HLF at pH 7.0 and 9.029.
OVOTRANSFERRIN is an underexploited yet potent natural protein with broad industrial applications. Contact us today to discuss how you can incorporate OVOTRANSFERRIN into your products.
- Potent antibacterial, antifungal, and antiviral properties
- Effective against gram-negative & gram-positive bacteria
- Binds free iron with high affinity, comparable to that of lactoferrin
- Industrially attractive bioactive properties of both native protein and derived peptides
- Iron carrier in physiological functional food supplements
- Antimicrobial component of edible protective films
- Prevention of fat-water separation in surfactant-free edible emulsions
- Reduction of mortality and antibiotic use in large-scale turkey farming operations
Regulations may vary according to the country. Always check the local legislation regarding the usage and claims of this product.
Our recommended review:
- Wu J & Acero-Lopez A: Ovotransferrin: Structure, bioactivities, and preparation | Publisher Site
- Valenti P et al.: Antibacterial activity of matrix-bound ovotransferrin. Antimicrob. Agents Chemother. 1982 | Publisher Site
- Valenti, P et al.: 1983. Importance of the presence of metals in the antibacterial activity of ovotransferrin. Ann. Ist. Super. Sanità 1983
- Ibrahim HR: Isolation and characterization of the bactericidal domain of ovotransferrin. Nippon Nogeikagaku Kaishi 1997
- Garibaldi JA: Role of microbial iron transport compounds in bacterial spoilage of eggs. Appl Microbiol. 1970 | Publisher Site
- Aguilera O et al.: Transferrins selectively cause ion efflux through bacterial and artificial membranes. FEBS Lett. 2003 | Publisher Site
- Valenti P et al.: Studies of the antimicrobial activity of ovotransferrin. Int. J. Tissue React. 1987 | Publisher Site
- Valenti P et al.: Antifungal activity of ovotransferrin towards genus Candida. Mycopathologia 1985. | Publisher Site
- Giansanti F et al.: Antiviral activity of ovotransferrin derived peptides. Biochem Biophys Res Commun. 2005 | Publisher Site
- Ibrahim HR et al.: Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim Biophys Acta. 2000 | Publisher Site
- Lee N et al.: One peptide derived from hen ovotransferrin as a pro-drug to inhibit the angiotensin-converting enzyme. Journal of Food and Drug Analysis. 2006 | Publisher Site
- Majumder L & Wu.: Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin, Food Chem. 2011 | Publisher Site
- Son M. et al.: Egg white ovotransferrin-derived ACE inhibitory peptide ameliorates angiotensin II-Stimulated insulin resistance in skeletal muscle cells, Mol. Nutr. Food Res. 2018 | Publisher Site
- Chen et al.: The utility of Ovotransferrin and Ovotransferrin-derived Peptides as Possible Candidates in the Clinical Treatment of Cardiovascular Disease. Oxidative Medicine and Cellular Longevity. 2017 | Publisher Site
- Shang N & Wu J: Egg White Ovotransferrin Shows Osteogenic Activity in Osteoblast Cells. J Agric Food Chem. 2018 | Publisher Site
- Shang N & Wu J: Egg White Ovotransferrin Attenuates RANKL-Induced Osteoclastogenesis and Bone Resorption. Nutrients. 2019 | Publisher Site
- Shang N et al.: Ovotransferrin Exhibits Osteogenic Activity Partially via Low-Density Lipoprotein Receptor-Related Protein 1 (LRP1) Activation in MC3T3-E1 Cells. J Agric Food Chem. 2020 | Publisher Site
- Ibrahim HR et al.: Ovotransferrin possesses SOD-like superoxide anion scavenging activity promoted by copper and manganese binding. Int J Biol Macromol. 2007 | Publisher Site
- Benedé S & Molina E: Chicken Egg Proteins and Derived Peptides with Antioxidant Properties. Foods 2020 | Publisher Site
- Ibrahim HR & Kiyono T: Novel anticancer activity of the autocleaved ovotransferrin against human colon and breast cancer cells. J Agric Food Chem. 2009 | Publisher Site
- Xie H et al.: Effects of ovotransferrin on chicken macrophages and heterophil-granulocytes. Dev Comp Immunol. 2002 | Publisher Site
- Ru Z et al.: Ovotransferrin exerts bidirectional immunomodulatory activities via TLR4-mediated signal transduction pathways in RAW264.7 cells. Food Science & Nutrition. 2021 | Publisher Site
- Seol KH et al.: Antimicrobial effect of κ-carrageenan-based edible film containing ovotransferrin in fresh chicken breast stored at 5°C Meat Sci. 2009 | Publisher Site
- Wei Z & Huang Q: Edible Pickering emulsions stabilized by ovotransferrin–gum arabic particles. Food Hydrocolloids. 2019 | Publisher Site
- Van Droogenbroeck C & Vanrompay D: Use of ovotransferrin on a turkey farm to reduce respiratory disease. Vet Rec. 2013 | Publisher Site
- Giansanti F et al.: The Nutraceutical Properties of Ovotransferrin and Its Potential Utilization as a Functional Food. Nutrients. 2015 | Publisher Site
- Galla R et al. Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model. Biomedicines. 2021 | Publisher Site
- Charter EA & Lagarde G: Lysozyme and Other Proteins in Eggs. Encyclopedia of Food Microbiology. 2014 | Publisher Site
- Hee Yeon Cho Ji-Eun Lee Jae HoonLee Dong UkAhn Kee-Tae Kim Hyun-DongPaik: Anti-biofilm effect of egg white ovotransferrin and its hydrolysates against Listeria monocytogenes 2022 | Publisher Site
- Qi Zeng, Yaping Liu, Jing Sun, Yongguo Jin: Providing New Insights on the Molecular Properties and Thermal Stability of Ovotransferrin and Lactoferrin | Publisher Site