EC Number   |
General Information |
Reference |
|---|
   3.4.22.33 | more |
comparative structural analysis of fruit and stem bromelain from Ananas comosus, structure homology modelling, model domain organisation, overview. The proteolytic fraction of pineapple stem is termed stem bromelain, while the one presents in the fruit is known as fruit bromelain (EC 3.4.22.33). NCBI conserved domain analysis reveals two domains of fruit and stem bromelain: cathepsin propeptide inhibitor (I29) and peptidase C1 |
753631 |
| 3.4.22.33 | more |
effects of bromelain on the pro-wound healing activities and the regenerative properties of mesenchymal stem cells, overview. The combination of bromelain and dexamethasone sodium phosphate induces a great activation of mesenchymal stem cells with an increase in hyaluronan and collagen production and antiinflammatory cytokines release, real-time polymerase chain reaction analysis of extracellular matrix proteins and remodeling enzymes in human mesenchymal stem cells, overview |
754265 |
| 3.4.22.33 | physiological function |
antiproliferative effect of bromelain from different tissues against B16F10 murine melanoma cells, overview |
-, 753890 |
| 3.4.22.33 | physiological function |
bromelain enzyme from pineapple fruit acts as an antiviral agent against HIV, hepatitis C and human papiloma virus. Patients are given two glasses of fresh juice from pineapple fruits per day resulting in reduced human immunodeficiency virus (HIV) load. Bromelain might cause some damage on the virus envelope protein structural components. Direct contact of bromelain enzymes from fruit powder with HI viruses causes morphological changes on the viruses |
754274 |
| 3.4.22.33 | physiological function |
bromelain is capable of unhairing of cow skin in solid state fermentation |
752429 |
| 3.4.22.33 | 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 |
754238 |
