Professor University of Alberta Edmonton, Alberta, Canada
Abstract: Food-derived bioactive peptides are increasingly recognized as food bioactives that can impart a wide range of health benefits. Bioactive peptides form one of the most complex and diverse groups of food bioactives in terms of both their structures and bioactivities. The potential health implication of bioactive peptides is being actively explored worldwide by many researchers and some have already been successfully marketed. The interest in these areas is burgeoning rapidly. Although bioactive peptides have been identified from many different food proteins, most research has been focused on animal proteins, especially dairy proteins, making many believe that animal proteins are better sources of bioactive peptides than plant proteins. Animal proteins are high quality and contain adequate and balanced amino acids, while most plant proteins are inferior in quality and “incomplete” in that they are deficient in one or more of the essential amino acids, and contain several antinutritional factors. This session aims to challenge this misbelief, and address the question of what makes a food protein a good source of bioactive peptides. The nutritional value of a food protein is largely based on the essential amino acid composition, where the significance of a food protein as a source of bioactive peptides is determined by the encrypted amino acid sequences. This session will showcase the presence of significant amino acid sequences within plant proteins with comparable or even better bioactives than those famous lactotripeptides, such as VPP and IPP. Understanding the presence of encrypted sequences with comparable or even better activity than animal proteins will provide a new way of valorization of plant proteins, especially those from byproducts, and represents a sustainable approach to prepare bioactive peptides from plant proteins.