Abstract
Milk can be considered one of the primary sources of nutrients for the mammalian neonate. Therefore, milk and milk-based products, such as infant formula, whey protein isolate, different varieties of cheese, and others are prepared to meet the nutritional requirements of the consumer. Due to its significant nutritional components and perishable nature, a variety of pathogenic microorganisms can grow and multiply quickly in milk. Therefore, various heat treatments can be employed for the improvement of the shelf life of milk. In comparison to pasteurized milk, due to excessive and severe heating, UHT milk has a more cooked flavor. During storage, changes in the physicochemical properties of milk can lead to off-flavors, undesirable browning, separation of fat, sediment formation, or gelation during the subsequent storage. Several important factors such as processing parameters, time-temperature abuse (storage condition), and packaging type also influence the quality characteristics and consumer acceptance of the milk; however, the influence of heat treatments on milk protein is inconstant. The major protein modifications that occur during UHT treatment are denaturation and aggregation of the protein, and chemical modifications of its amino acids. These UHT-induced protein alterations can change digestibility and the overall biological influence of the intake of these proteins. Therefore, this review is focused on the influence of UHT on the physicochemical and structural attributes of milk proteins during storage. There are many indications of milk proteins present in the UHT milk, and milk products are altered during processing and storage.
Highlights
Introduction iationsMilk is a complex biological fluid, produced in the mammary gland of female mammalian species
Immunoglobulins are the most heat-sensitive whey proteins, which are followed by bovine serum albumin (BSA), βlactoglobulin (β-Lg), α-lactalbumin (α-La), and proteose peptones, though the last are not affected by heat
Ultra-high temperature (UHT)-treated milk is a successful method to extend the shelf-life of milk and its products
Summary
Milk contains approximately 3.5% by weight protein, which is a highly complex system. This milk protein is usually divided into two main fractions based on their solubility nature. Proteins are made up of a polypeptide chain of amino acid residues joined together by peptide bonds and cross-linked by disulfide bonds. The three-dimensional arrangement of amino acid residues that are close to each other in the linear sequence is referred to as a secondary structure. The tertiary structure refers to the spatial arrangement of amino acid residues that are wide apart in the linear sequence, allowing for more folding and coiling to occur [16]. The milk proteins include αs1 -casein, αs2 -casein, β-casein, κ-casein, α-lactalbumin (αLA), and β-lactoglobulin (βLG), which are the main components of milk and whey products
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