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Nanoencapsulation Methods In Iron Fortification of Dairy Food Matrices
Published in Megh R. Goyal, Santosh K. Mishra, Lohith Kumar Dasarahalli-Huligowda, Nanotechnology Applications in Agricultural and Bioprocess Engineering, 2021
Human milk contains iron 6.8 mmol L–1 and 9.3 mmol L–1 in milk and colostrum, respectively in a complex form with lactoferrin [50]. Lactoferrin is a glycoprotein that plays an important role in the human innate immune system. In human milk, lactoferrin is an iron-free apoprotein that can bind two ferric ions. Human milk contains citrate, which facilitates lactoferrin binding to iron. It is the most dominant whey protein in human milk. Lactoferrin is present in high quantities in colostrum and declines over time. Lactoferrin is resistant to proteolysis, especially in its iron-saturated form. Lactoferrin has high affinity towards iron and increases in the weak acidic medium.
Spray Drying of Dairy and Cereal Food Products
Published in M. Selvamuthukumaran, Handbook on Spray Drying Applications for Food Industries, 2019
Whey contains major proteins, such as α-lactalbumin, β-lactoglobulin, and lactoferrin (Kumar et al., 2008). Lactoferrin has a lot of bioactive properties, such as, antibacterial activity, anti-inflammatory activity, etc. It has the property of binding well with iron (Darewicz et al., 2014).
Production and characterization of infant milk formula powders: A review
Published in Drying Technology, 2021
A. K. M. Masum, Jayani Chandrapala, Thom Huppertz, Benu Adhikari, Bogdan Zisu
Ingredients such as lactoferrin, milk fat globule membrane (MFGM), probiotics, and prebiotics are added in IMF products due to their specific health benefits to infants. MFGM is a glycoprotein-phospholipid tri-layer that covers the fat droplets in fresh bovine milk. Lactoferrin is an iron-binding whey protein which is found in both human and bovine milk, and possesses antimicrobial, anti-inflammatory, and immunological functions. The concentration of this protein is higher in human milk (varies from 1 mg/mL in mature milk to 7 mg/mL in colostrum) than bovine milk (0.02–0.2 mg/mL).[31] Lactoferrin was successfully added in IMF formulations,[32] and the formulas were safe, well-tolerated, and associated with normal growth pattern.[33]
Surface properties and adsorption of lactoferrin-xanthan complex in the oil-water interface
Published in Journal of Dispersion Science and Technology, 2020
Rui Fan, Tianxing Zhang, Kedong Tai, Fang Yuan
Milk proteins are natural vehicles for bioactive components and their structural and physicochemical properties facilitate their functionalities in delivery systems.[17] Lactoferrin (LF) has attracted strong interest as a functional bioactive ingredient for applications in food and pharmaceutical products. LF is a monomeric, globular and iron-binding glycoprotein with the molecular mass around 80 kDa and 680 amino acids residues. Due to the higher positive charges on the molecule surface, LF has an isoelectric point (pI) about 8.5. Thus, the electrostatic interaction between LF and XG has been harnessed to form various particulate systems and modulate emulsion functionality over a wide pH range.[18,19] It was reported that the interactions occurring between LF and XG are influenced by their surface charge, therefore, an investigation of the interfacial behavior is very useful for the functional food industry.[13]
Spontaneous interaction of lactoferrin with casein micelles or individual caseins
Published in Journal of the Royal Society of New Zealand, 2018
Lactoferrin is a glycoprotein found in the whey of mammalian milk. It is in relatively low concentrations in bovine milk (c. 0.2 mg/mL) but at higher levels in bovine colostrum (c. 1.5 mg/mL). Lactoferrin is found at much higher levels in human milk (c. 1 mg/mL) and human colostrum (up to 7 mg/mL). Lactoferrin has a molecular weight of c. 80 kDa, and is a single polypeptide chain of c. 673 amino acids folded in such a way to produce two homologous domains, with each domain having an iron binding centre. When iron (in ferric form) is bound to lactoferrin, it is accompanied by a bicarbonate molecule to offset the positive charge of the ferric ion. Lactoferrin has a high affinity for ferric ions over a wide pH range, but in its natural state in milk the iron binding capacity is usually 15% of saturation or less (Kanyshkova et al. 2001; Lonnerdal 2003). Natural freeze-dried lactoferrin or its solutions are light pink in colour. Iron depleted apo-lactoferrin is colourless whereas iron saturated holo-lactoferrin is blood red. Lactoferrin has two potential glycosylation sites, but, like κ-casein, the level of glycosylation varies, and as a consequence so does the molecular weight of lactoferrin, which affects its separation characteristics by techniques such as HPLC or electrophoresis. Details on the extent and nature of the glycosylation of lactoferrin have been reported (Kanyshkova et al. 2001; Lonnerdal 2003).