ABSTRACT
Many of the properties of food proteins with physiological significance beyond the nutritional requirements of nitrogen for growth and maintenance are attributed to physiologically active peptides encrypted in the proteins.1 Within the sequence of the parent protein the peptides are inactive but during in vivo gastrointestinal digestion or in vitro enzyme treatment and food processing, bioactive peptides or “food hormones” are released. Depending on the amino acid sequence, the peptides exhibit various functions such as opioidergic, immunostimulatory, antihypertensive, and antimicrobial activity.2,3 A number of peptides with different biological activities have been described4 since the discovery in 1970 of bradykinin-potentiating peptides possessing angiotensin 1-converting enzyme (ACE)-inhibitory activity.5,6 The observation that functional peptides can be generated through proteolytic digestion of a parent protein, which may have a different physiological function in the organism, suggests that multifunctionality may be an intrinsic property of most proteins, and that bioactive peptides can be “tailored and modeled” to achieve a desired function.7
