Bromelain (pineapple)

Synonym(s): pineapple, bromelain, Proteolytic enzymes

Nutrient group: plant extracts & active ingredients, Enzymes

Sources and physiological effects

Dietary sources
The pineapple belongs to the Bromeliaceae family and is originally native to South America. Nowadays, pineapples are cultivated in tropical areas all over the world. A large amount is processed for tinned food and to a lesser extent, the fruit is consumed as fresh fruit. Production waste is partly used as animal feed for ruminants and pigs. The sems also serve to produce the proteolytic enzyme bromelain. Bromelain is used in the food industry to make meat and gelatine softer. However, it is also used in complementary medicine and is increasingly offered in the form of dietary supplements and dietary foods.
Physiological effects
Gastrointestinal tract	Bromelain is a cysteine protease.
Wound healing and inflammation	Bromelain promotes the conversion of plasminogen to plasmin and thus increases fibrinolysis. Bromelain cleaves bradykinin and thereby reduces vascular permeability, which in turn reduces the amount of inflammatory mediators and water entering tissues (decongestant effect).
Tumor defense	Bromelain increases monocyte activity against tumor cells. Bromelain increases the production of cytokines (TNF-α, IL-1β, IL-6, IL-8).

Detailed information

Enzymes promote wound healing

Enzymes are vegetable or animal protein compounds that act as biocatalysts and enable or accelerate certain processes without being modified themselves.
Bromelain is a natural proteolytic enzyme from pineapple that accelerates wound healing processes and reduces swelling by degrading and eliminating necrotic tissue residues (1). The natural biocatalysts contained in the pineapple are used for enzymatic wound cleansing, but do not attack the intact epithelial, granulation and muscle tissue (1). Proteolytic enzymes are mainly used for secondarily infected wounds, abscesses, burns, frostbite, sports injuries and surgical procedures (2).
Since enzymes also have antithrombotic properties, enzyme therapy should only be used after surgery when hemostasis is assured.

Acute and chronic inflammation

Proteolytic enzymes such as bromelain regulate and modulate inflammatory processes. They are an efficient therapeutic for acute and chronic inflammation. The use of proteolytic enzymes is particularly successful in the treatment of chronic inflammation of the respiratory tract and inflammation of muscles and tendons. Proteases accelerate the inflammatory process by disposing of necrotic tissue residues and have pain-relieving properties due to their anti-edemic properties (3). In children, enzymes are also successfully used as an adjuvant therapy for bronchitis and sinusitis (4) (5).

Sport injuries and trauma

Proteolytic enzymes have proven to be an effective supplement to conventional treatments in the post-traumatic phase after injuries such as bruises, strains and sprains. Especially in acute therapy, the anti-edematous and fibrinolytic effects are scientifically supported (6).
Post-traumatic swelling after surgery can also be reduced significantly faster through enzyme administration, which also noticeably reduces pain (7).

Adjuvant use in radiation and chemotherapy

Oncology is another field of application for proteolytic enzymes. The targeted use of enzyme combinations can significantly reduce the negative side effects of chemo- and radiation treatment (8) and improve the symptoms of tumor disease as well as increase the quality of life and chances of survival (9). This has been demonstrated in clinical studies in patients with colon tumors (10). The activity of macroglobulin alpha-2-M, which is enhanced by proteolytic enzymes, is assumed to be the basic biochemical mechanism. Alpha-2-M ca irreversibly inactivate TGF-beta fractions in serum. TGF-beta concentrations are greatly increased in certain tumor diseases (11) (12).

Support digestive performance

Bromelain can also be used as a proteolytic enzyme to aid digestion. The enzymes promote the dissolution of protein residues from food. Bromelain is therefore particularly suitable for supporting digestion in states of limited digestive capacity such as in pancreatic insufficiency.

Biological enzyme activity: F.I.P. and U.S.P.

Biological activity is decisive for the therapeutic efficiency of the enzymes. This is expressed in F.I.P. units or in U.S.P. units. F.I.P. stands for Fédération International Pharmaceutique, U.S.P. for United States Pharmacopoeia. These units correspond to defined enzyme quantities, which convert 1 µmol defined substrate in a certain time under standard conditions.

Indications

Effect	Indication	Dosage
Physiological effects at a low intake	Wound healing disorders and chronic wounds such as open legs, decubitus, diabetic foot	300 mg/d
	For acute injuries & burns, such as extensive abrasions, bruises, strains	300 mg/d
	For dietary support of wound healing in the jaw, nose, & sinus area after surgery	300 mg/d
	For acute inflammations e.g. of the veins, respiratory organs, sinuses and maxillary sinuses (colds & flu infections), tendons, muscles	300 mg/d
	Therapy support for persistent and painful chronic inflammation (e.g. tennis elbow)	300 mg/d
	Adjuvant therapy for tumor treatment and for chemo and radiotherapy	300 mg/d
	For complaints of the upper abdomen and dyspeptic diseases caused by limited digestive performance, especially in older patients or in diabetics with endogenous and exogenous pancreatic insufficiency	150 - 300 mg/d

Administration

General mode of administration
When	Bromelain should be taken immediately before meals to support digestive performance. To improve wound healing and inflammatory processes bromelain should be taken fasting or 1 hour before a meal.
Side effects
No side effects are known to date.
Contraindications
Due to its antithrombotic properties, enzymes should be used after surgery only if hemostasis is assured.

Interactions

Drug interactions
None	No interactions known to date
Nutrient interactions
Enzymes	Bromelain seems to improve the anti-inflammatory effect of quercetin.
Glucosamine and chondroitin	A combination can support anti-inflammatory therapy for joint diseases.

References

1) Maurer, H. 2001. Bromelain: biochemistry, pharmacology and medical use. Cellular and Molecular Life Sciences 58, Nr. 9: 1234–1245. doi:10.1007/pl00000936.

2) Koller, J. et al. 2009. Enzymatic necrolysis of acute deep burns—Report of preliminary results with 23 patients. Burns 35. doi:10.1016/j.burns.2009.06.142.

3) Veremeenko, K. et al. 2000. The mechanisms of the curative action of systemic enzyme therapy. Lik Sprava. (2):3-11.

4) Lanchava, N. et al. 2005. Wobenzym in treatment of recurrent obstructive bronchitis in children. Georgian Med News. (127):50-3.

5) Braun, J. M. et al. 2005. Therapeutic use, efficiency and safety of the proteolytic pineapple enzyme Bromelain in children with acute sinusitis in Germany. In Vivo. 19(2):417-21.

6) Berg, A. et al. 2005. Bromelain - Übersicht und Diskussion zur therapeutischen Anwendung und seiner Bedeutung in der Sportmedizin und Sporttraumatologie. Deutsche Zeitschrift für Sportmedizin. 56(1):12-19.

7) Ordesi, P. et al. 2014. Therapeutic efficacy of bromelain in impacted third molar surgery: a randomized controlled clinical study. Quintessence Int. 45(8):679-84.

8) Leipner, S. 2000. Systemic Enzyme Therapy in Oncology. Drugs 59, Nr.4:769–780. doi:10.2165/00003495-200059040-00004.

9) Beuth, J. 2008. Proteolytic Enzyme Therapy in Evidence-Based Complementary Oncology: Fact or Fiction? Integrative Cancer Therapies 7, Nr. 4 (January): 311–316. doi:10.1177/1534735408327251.

10) Popiela, T. et al. 2001. Influence of a complementary treatment with oral enzymes on patients with colorectal cancers – an epidemiological retrolective cohort study. Cancer Chemotherapy and Pharmacology 47 (January). doi:10.1007/s002800170010.

11) Desser, L. et al. 2001. Oral therapy with proteolytic enzymes decreases excessive TGF-β levels in human blood. Cancer Chemotherapy and Pharmacology 47 (January). doi:10.1007/s002800170003.

12) Lauer, D. et al. 2001. Modulation of growth factor binding properties of a2-macroglobulin by enzyme therapy. Cancer Chemotherapy and Pharmacology 47 (January). doi:10.1007/s002800170002.

References Interactions:

Stargrove, M. B. et al. Herb, Nutrient and Drug Interactions: Clinical Implications and Therapeutic Strategies, 1. Auflage. St. Louis, Missouri: Elsevier Health Sciences, 2008.

Gröber, U. Mikronährstoffe: Metabolic Tuning –Prävention –Therapie, 3. Auflage. Stuttgart: WVG Wissenschaftliche Verlagsgesellschaft Stuttgart, 2011.

Gröber, U. Arzneimittel und Mikronährstoffe: Medikationsorientierte Supplementierung, 3. aktualisierte und erweiterte Auflage. Stuttgart: WVG Wissenschaftliche Verlagsgesellschaft Stuttgart, 2014.