Beta Lactoglobulin F, also known as β-Lactoglobulin F or B-lg F, is a variant of the beta-lactoglobulin protein found in the milk of many mammalian species, including cows. It belongs to the lipocalin family of proteins and is primarily synthesized in the mammary gland.
Beta-lactoglobulins are heat-stable proteins that act as carriers of hydrophobic molecules, such as vitamins and fatty acids. The F variant of beta-lactoglobulin is a naturally occurring genetic variant that differs from the A variant by a single amino acid substitution at position 64, where phenylalanine (F) replaces histidine (H).
Beta Lactoglobulin F accounts for a significant proportion of the total beta-lactoglobulin present in cow's milk. It is primarily associated with the transport and protection of hydrophobic ligands, as well as being involved in important physiological functions such as regulating milk osmolarity and promoting the formation of stable emulsions.
Due to its structure and properties, Beta Lactoglobulin F has been of great interest in various fields, including food and pharmaceutical industries. It is extensively studied for its functional and nutritional properties, including its role in protein digestion, allergenicity, and potential therapeutic applications. Additionally, it is widely used as a marker for monitoring and authenticating the source of milk and dairy products.
In conclusion, Beta Lactoglobulin F is a variant of the beta-lactoglobulin protein found in milk, primarily synthesized in the mammary gland. It plays a crucial role in the transport and protection of hydrophobic ligands and has been extensively studied for its functional, nutritional, and commercial significance.
