Physiological significance, structure and isolation of α-lactalbumin

Abstract

Along with the constant increase in the cheese milk production, the world whey production is increasing constantly too (>2 % per year). The excellent nutritional properties attributed to whey are mainly conditioned by the presence of highly valuable proteins with wide range of biological and functional properties. The main whey proteins are β-lactoglobulin (β-Lg) and α-lactalbumin (α-La) which are extensively used in functional foods and beverages, infant formulas, sport diets, but are a very good source of bioactive peptides too. Along with casein, β-Lg is most commonly made responsible for causing food allergies, especially in infants whose digestion system isn’t completely developed. Hence, there is a great interest for removing β-Lg prior to whey utilization in certain products. At the same time α-La was recognized as the nutritionally most valuable protein and might be regarded as an ideal ingredient for infant formulas. Thus, the aim of the present paper was to give an overview of the currently available methods for α-La isolation, and to highlight their advantages and disadvantages as well. Also, this paper reviews the most recent insights related to the structure and physiological significance of α-La.