AFP Peptizyde was developed in response to parents request for a high DPP IV-containing enzyme product that did not include fruit-based enzymes such as papain or bromelain. Like Peptizyde, it is a combination of three different proteolytic enzymes isolated from fungal plant sources. Each enzyme has a unique set of peptide bonds it prefers to break, so the combination of these enzymes allows much more efficient means of quickly and thoroughly breaking down (hydrolyzing) proteins to its smaller components. The enzymes in AFP Peptizyde work only on food proteins, not carbohydrates, fats, or other compounds, and do not interfere with medications or other supplements (unless they are also proteins, which is extremely unlikely). AFP Peptizyde may be used in combination with other enzyme products, such as HN-Zyme Prime and or No-Fenol. One would use either Peptizyde or AFP Peptizyde for protein digestion based on 1) known sensitivities to papain or, 2) a child objecting to the odor of Peptizyde (which is due to the presence of papain).
The aminopeptidase enzyme dipeptidyl peptidase IV, or DPP IV, is able to hydrolyze and inactivate the exorphin peptide, casomorphin. However, for maximal protein breakdown, it is not useful alone, and should be combined with other proteases with different and less stringent peptide bond specificity. For this reason, AFP Peptizyde also contains two other fungal proteases with high activity in acid conditions. These enzymes are present in AFP Peptizyde in high amounts for the purpose of quickly hydrolyzing proteins while the food is still in the stomach. The ability of AFP Peptizyde enzymes to withstand the low pH of the stomach and remain active under acidic conditions allows hydrolysis of casein and gluten prior to entrance into the small intestine. Casein and gluten, in the presence of pancreatic enzymes in the duodenum, can produce exorphin peptides that may be readily absorbed from the intestine (these peptides are not absorbed from the stomach). AFP Peptizyde supplements the "normal" hydrolysis of casein, gluten, and other food proteins such that the exorphin peptides are not produced because the specific cleavage pattern to produce these peptides is altered.