Bromelain is a complex of proteolytic enzymes derived from the Ananas comosus (pineapple) plant, primarily extracted from the stem and fruit. As a thiol endopeptidase, bromelain hydrolyzes a wide variety of protein substrates and remains active over a broad pH and temperature range. Due to its multifaceted biochemical properties, bromelain is widely used in biomedical research, biotechnology, food processing, and pharmaceutical applications.
Bromelain
| CAS No: | 9001-00-7 |
| EINECS No: | 232-627-2 |
| EC No: | 3.4.22.32 |
| Synonyms: | Ananase, Pineapple Protease, Bromelin |
Product Summary
Function
Bromelain catalyzes the cleavage of internal peptide bonds in proteins, exhibiting broad specificity for substrates containing lysine, alanine, and glycine residues. It also possesses secondary activities such as:
- Fibrinolytic, anticoagulant, and anti-inflammatory effects
- Phosphatase, glucosidase, and peroxidase activities (minor)
- Optimal pH: 5.5 – 7.5
- Optimal Temperature: 45°C – 55°C
- Enzyme Type: Cysteine protease
- Inhibitors: E-64, iodoacetamide, and heavy metal ions
Mechanism of Action
Bromelain acts via a catalytic dyad involving a cysteine and a histidine residue. The enzyme forms a transient covalent intermediate with the target peptide bond, followed by hydrolysis and product release. This thiol-based mechanism is shared with other members of the papain-like protease family.
Applications in Scientific Research
- Protein digestion for proteomics and enzymatic profiling
- Anti-inflammatory studies: Bromelain is frequently studied for its effects on cytokines, prostaglandins, and immune modulation
- Model for cysteine protease studies in enzymology and drug development
- Cell dissociation for tissue culture in gentle proteolysis applications
Packaging & Storage
- Available as lyophilized, slightly yellow-brown powder
- Store at 2–8°C (powder); –20°C recommended for long-term preservation
References
- Maurer HR. 2001: Bromelain: biochemistry, pharmacology and medical use , Cell Mol Life Sci. 58(9):1234-45.
- Tochi BN, 2008: Therapeutic application of pineapple protease , Pakistan J Nutrition. 7(4):513-20.
- Hale LP. 2004: Proteolytic activity and immunogenicity of oral bromelain within the gastrointestinal tract of mice., Inter Immunopharm. 4(2):255-64.
- Bhattacharyya BK. 2008: Bromelain: an overview., Nat Product Radiance. 7(4):359-63.
- Rowan AD, Buttle DJ. 1994: Pineapple cysteine endopeptidases., Meth Enzymol. 244:555-68.
- Hale LP, Haynes BF. 1992: Bromelain treatment of human T cells removes CD44, CD45RA, E2/MIC2, CD6, CD7, CD8, and Leu 8/LAM1 surface molecules and markedly enhances CD2-mediated T cell activation., J Immunol. 149(12):3809-16.
- Leipner J, et al. 2002: Therapy with proteolytic enzymes in rheumatic disorders., BioDrugs. 15(12):779-89.
- Bhui K, et al. 2009: Bromelain inhibits COX-2 expression by blocking the activation of MAPK regulated NF-kappa B against skin tumor-initiation triggering mitochondrial death pathway. , Cancer Letters. 282(2):167-76.
- Huang JR, et al. 2008: Bromelain inhibits lipopolysaccharide-induced cytokine production in human THP-1 monocytes via the removal of CD14., Immunological Investigations. 2008;37(4):263–277.
- Varilla C, et al. 2021: Bromelain, a group of pineapple proteolytic complex enzymes (Ananas comosus) and their possible therapeutic and clinical effects. A summary., Foods. 10(10):2249.
- Chobotova K, et al. 2010: Bromelain’s activity and potential as an anti-cancer agent: current evidence and perspectives., Cancer Letters. 290(2):148-56.