0210114210
0210114280
0210114290
0210114291
0210114225
IC10114210EA
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IC10114210
IC10114280
IC10114290
IC10114291
IC0210114225
Pineapple Bromelain, MP Biomedicals
Enzymes
Bromelain is a glycoprotein which is a highly active thiol proteinase (non-specific cysteine protease), which splits glycine esters but not lysine esters; it is also a protein-digesting and milk-clotting enzyme. Substrates susceptible to bromelain include all of the common protein materials such as gelatin, casein, gluten, collagen, elastin, globulins and muscle fiber protein.
- Presentation: Tan Powder
- Isoelectric point (pl): 9.551
- 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.
- Readily soluble in water, insoluble in most organic solvents such as acetone, ether, ethanol and methanol.
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.
Bromelain is a cysteine endopeptidase with broad specificity for cleavage of proteins. Bromelain may be from a stem or piece of fruit.
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-.
Unit Definition (GDU): One unit will hydrolyze 1.0 mg of amino nitrogen from gelatin in 20 minutes at pH 4.5 at 45 °C.