Different Approaches to Improve Thermostability of Whey Proteins: A Review

Abstract

Whey proteins constitute 20% of the proteins in milk and include β-lactoglobulin (β-Lg; approximately 3.2 g/L), αlactalbumin (α-La; approximately 1.2 g/L), bovine serum albumin (BSA; approximately 0.4 g/L), and immunoglobulins (approximately 0.7 g/L) (Raikos, 2010). Whey protein is considered as high quality protein because of its branch chain amino acid. Growing awareness about the nutritional benefits of whey proteins and technological advancements in improving functional properties has led to an ever increasing demand of whey proteins in the form of commercial whey protein ingredients, such as whey protein concentrates (WPC) and whey protein isolates (WPI). Whey protein ingredients are widely used in a variety of products, such as whey protein fortified sports beverages, nutritional and meal replacement as well as medical and clinical nutrition beverages (Suresh and Hasmukh, 2017). Whey protein isolates (WPI) and whey protein concentrate (WPC) are used as food ingredients due to their commercially important functional properties such as solubility, viscosity, water-holding capacity, International Journal of Current Microbiology and Applied Sciences ISSN: 2319-7706 Volume 8 Number 04 (2019) Journal homepage: http://www.ijcmas.com