Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ananas comosus | O23791 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme partially from ripe fruits by lyophilization and gel filtration | Ananas comosus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fruit | - |
Ananas comosus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
azocasein + H2O | - |
Ananas comosus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Ananas comosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Ananas comosus |
General Information | Comment | Organism |
---|---|---|
physiological function | small peptides are separated from larger peptides and proteins by fruit bromelain in the human digestive tract, the peptides are capable of destabilizing and desaggregating insulin aggregates (e.g. B23-B30 des-octapeptide) to oligomers. The peptides GG and AAA serving as negative controls show no potency in destabilization of aggregates. Disaggregation potency of the peptides wis also observed when insulin is deposited on Hep-G2 liver cells where no formation of toxic oligomers occurs. Deposition of insulin aggregates in human body leads to dysfunctioning of several organs. Amyloidogenic des-octapeptide (B23-B30 of insulin) incapable of cell signaling also show cytotoxicity similar to insulin. This toxicity can also be neutralized by bromelain derived peptides. Disaggregated insulin has a structure distinctly different from that of its hexameric (native) or monomeric states, FT-IR and far-UV circular dichroism analysis. Ability of auto digested peptides from bromelain to act as an inhibitor of amyloid formation | Ananas comosus |