Bromelain is a cysteine endopeptidase with broad specificity for cleavage of proteins. Bromelain may be from a stem or piece of fruit.
- Glycoprotein which is a highly active thiol proteinase
- Non-specific cysteine protease
- Splits glycine esters but not lysine esters
- Protein digesting and milk-clotting enzyme
Bromelain may be used to inhibit the biosysnthesis of proinflammatory prostaglandins. It may be used to reduce clotting efficiency. Bromelain, from pineapple stem, has been used to make enzymatic hydrolysates of honeybee-collected pollen.
Specific Activity: 1100-1500 GDU/gram
Product Type: Proteins, Enzymes & Peptides
Presentation: Tan Powder
Format: Powder
Isoelectric point (pI): pI: 9.551
pH: Bromelain is stable at pH 3.0 to 6.5 and once it has combined with its substrate, the activity is no longer susceptible to the effect of the pH. (Lit.)
NOTES: Activators: Bromelain can be activated by cysteine, bisulfite salt, NaCN, H2S, Na2S and benzoate; however, bromelain is usually sufficiently active without the addition of activators. Generally, if bromelain loses an appreciable amount of its activity by undue storage or preparation conditions, the enzyme can be markedly reactivated by cysteine. Inhibitors: Bromelain is inhibited by Hg2+, Ag+, Cu2+, α-1-antitrypsin, estatin A & B, Iodoacetate, TLCK, TPCK. Preferential Cleavage: Lys-, Ala-, Tyr-, Gly-
Solubility: Readily soluble in water, insoluble in most organic solvents such as acetone, ether, ethanol and methanol.
Storage & Handling Store at -20°C.