Widening potentials of whey proteins and a look towards unexplored application fields

Whey proteins (WPs) are recovered by cheese whey or other dairy industry by-products (ricotta or scotta) through sophisticated strategies promoting their conversion into high value-added products to accrue valorisation of the final product [1]. Due to the high nutritional value and specific functional properties, these products are employed both in the food and pharmaceutical industries for different applications/purposes [2,3]. Recently, great interest has been devoted to WP derived peptides for their well-known biological activities. Bioactive peptides are amino acid sequences that are encrypted within the native structure of proteins, which required hydrolysis for their release. Biological activities such antimicrobial, hypocholesterolemic, antioxidant, angiotensin converting enzyme (ACE)- inhibitor, opioid-like have been explored by in vitro and in vivo studies [4]. In this note the biological activities of WP derived peptides obtained by enzymatic hydrolysis, will be presented and discussed along with the exploitation of bioinformatic tools on line available, and a summary of applications in food or clinical sector will be also illustrated. Special attention will be placed on antimicrobial and antibiofilm peptides obtained by lactoferrin hydrolysis followed by characterization and identification by LC-MS/ MS of the peptide fractions endowed with biological activities, part of which was assayed in fresh foods (dairy products and ready to eat vegetables) to improve their shelf life under storage conditions [5-9]; other applications of the identified bioactive peptides as a control strategy against skinborne staphylococcal biofilms will be also illustrated paving the way for interesting future applications in cosmetic formulation for skin care [10]. We herein report how the use of complementary experimental and theoretical investigations allowed the identification of novel angiotensin converting enzyme (ACE) inhibitory peptides obtained from a WP hydrolysate and addressed the rational design of even shorter sequences based on molecular pruning [11]. The identified peptides (IAEK, IPAVF, MHI), endowed with high ACE inhibitory activity proved also to be promising for their antiviral activity against the SARS-CoV-2 3C-like protease (3CLpro) and Human Rhinovirus 3C protease (3Cpro) highlighting the high value of WP derived peptides for performing multitarget studies [12]. The herein presented studies highlight the high potential of WP derived peptides as promising molecules to be exploited in the development of target-specific or multi-target agents in pharmaceutical sectors and as unexplored preservatives in food sectors.