“…Not all food proteins are digested, absorbed, and utilized to the same extent because of inherent differences in their source (e.g., inside vegetable cells with indigestible membranes), their physicochemical nature (e.g., protein configuration and AA binding), the presence of food constituents that modify digestion (e.g., dietary fiber, tannins, and other polyphenols), the presence of antinutritional factors that interfere with protein breakdown (e.g., trypsin inhibitors and lectins), and processing conditions that alter the nature or release of AAs (e.g., Maillard reaction and formation of polyAAs and methylmercaptan) ( 2 , 8 ). Protein nitrogen digestibility values and more recently ileal AA digestibility values of specific foods and well-defined diets may be taken from reliable published data or must be determined, preferably in humans ( 3 ).…”