The Multifaceted Roles of Bovine Lactoferrin: Molecular Structure, Isolation Methods, Analytical Characteristics, and Biological Properties

Bovine lactoferrin (bLF) is widely known as an iron-binding glycoprotein from the transferrin family. The bLF molecule exhibits a broad spectrum of biological activity, including iron delivery, antimicrobial, antiviral, immunomodulatory, antioxidant, antitumor, and prebiotic functions, thereby making it one of the most valuable representatives for biomedical applications. Remarkably, LF functionality might completely differ in dependence on the iron saturation state and glycosylation patterns. Recently, a violently growing demand for bLF production has been observed, mostly for infant formulas, dietary supplements, and functional food formulations. Unfortunately, one of the reasons that inhibit the development of the bLF market and widespread protein implementation is related to its negligible amount in both major sources─colostrum and mature milk. This study provides a comprehensive overview of the significance of bLF research by delineating the key structural characteristics of the protein and elucidating their impact on its physicochemical and biological properties. Progress in the development of optimal isolation techniques for bLF is critically assessed, alongside the challenges that arise during its production. Furthermore, this paper presents a curated list of the most relevant instrumental techniques for the characterization of bLF. Lastly, it discusses the prospective applications and future directions for bLF-based formulations, highlighting their potential in various fields.