Papain (Papaya)

Synonym(s): papain

Nutrient group: plant extracts & active ingredients, Enzymes

Sources

Dietary sources

The papaya tree belongs to the family of melon trees (Caricaceae) and originates from the tropics of America. Today it is cultivated worldwide in tropical and subtropical areas. The seeds of the papaya fruit are very rich in papain, a proteolytic enzyme used, among other things, to tenderize meat. The fruit can be processed unripe like a vegetable and is used in traditional dishes of the tropics. The ripe fruit is sweet and available in worldwide.

Detailed information

Acute and chronic inflammation

Proteolytic enzymes such as papain regulate and modulate inflammatory processes. They are an efficient therapeutic for acute and chronic inflammation (1). 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 course of the inflammatory process by disposing of necrotic tissue residues and have an analgesic effect due to their anti-edemic properties (2).. Enzymes have also been successfully used as an adjuvant treatment for bronchitis and sinusitis in children (3) (4).

Sport injuries and traumatological injuries

Proteolytic enzymes have proven to be an effective supplement to conventional therapies in the post-traumatic phase after injuries such as bruises, strains, sprains. Especially in acute therapy the anti-edematous and fibrinolytic effects are scientifically demonstrated (5).
Post-traumatic swelling after surgery can also be reduced significantly faster through enzyme administration, which also noticeably reduces pain (6).

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 (7) and improve the symptoms of a tumor disease as well as increase the quality of life and chances of survival (8). This has been demonstrated in clinical studies in patients with colon cancer (9). The activity of macroglobulin alpha2M, which is enhanced by proteolytic enzymes, is assumed to be the basic biochemical mechanism. Alpha2M can irreversibly inactivate TGF-beta fractions in serum. TGF-beta concentrations are greatly increased in certain tumor diseases (10) (11).

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 Internationale Pharmaceutique, U.S.P. for United States Pharmacopeia. 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 sinus and nasal area after surgery	300 mg/d
	For acute inflammation e.g. of the veins, respiratory organs, sinuses and maxillary sinuses (colds & flu infections), tendons, muscles	300 mg/d
	Therapeutic support for persistent and painful chronic inflammation (e.g. tennis elbow)	300 mg/d
	Complementary therapy for cancerand for chemo and radiotherapy	300 mg/d
	For complaints of the upper abdomen and dyspeptic diseases caused by impaired 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	To support the digestive tract, papain should be taken just before meals. To improve wound healing and inflammatory processes, papain 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 or nutrient interactions
None	No relevant interactions are known to date.

Further information

Proteolytic Enzymes: Adjuvants for a strong immune system

Enzymes are biocatalysts of life. They accelerate biological reactions and are basic co-factors for all biochemical processes in the body. More than 5000 different enzymes are currently described in the human organism. Hydrolases have been in the focus of modern research for many years. The physician Prof. Wolf and the biologist Dr. Karl Ransberger first identified proteases at the beginning of the 1950s, i.e. enzymes that cleave protein compounds under hydrolysis. When these proteases, such as bromelain from the pineapple, papain from the papaya or trypsin/chymotrypsin from the pancreas, were released into the bloodstream of animals that previously had injuries with inflammatory reactions, they healed significantly faster. This finding was the birth of systemic enzyme therapy. Research on the pharmacokinetic and pharmacodynamic behavior of enzymes formed the basis for the establishment of a completely new form of therapy, which is used by over 2 million patients a year in Germany alone today. READ MORE < >

Systemic enzymes in sports medicine

The use of proteolytic enzymes such as bromelain, papain, trypsin and chymotrypsin is of great importance in sports medicine. Due to the consistent positive experiences, which are also supported step by step by new scientific evidence, systemic enzyme therapy has gained a firm place as a complementary therapy option. Whether as an immediate measure for acute injuries, as a long-term therapy for chronic muscle, tendon or joint complaints or for supportive use during heavy training in top-class sport, proteolytic enzymes are effective helpers free of side effects and highly accepted by patients. READ MORE <

References

1) Koller, J. et al. 2008. Enzymatic necrolysis of acute deep burns - report of preliminary results with 22 patients. Acta Chir Plast. 50(4):109-14.
2) Veremeenko, K. N. et al. 2000. The mechanisms of the curative action of systemic enzyme therapy. Lik Sprava. (2):3-11.
3) Lanchava, N. et al. 2005. Wobenzym in treatment of recurrent obstructive bronchitis in children. Georgian Med News. (127):50-3.
4) 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.
5) 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.
6) Kamenícek, V. et al. 2001. Systemic enzyme therapy in the treatment and prevention of post-traumatic and postoperative swelling. Acta Chir Orthop Traumatol Cech. 68(1):45-9.
7) Leipner, J., Saller, R. 2000. Systemic enzyme therapy in oncology: effect and mode of action. Drugs. 59(4):769– 80.
8) Hubarieva, H. O. et al. 2000. Systemic enzymotherapy as a method of prophylaxis of postradiation complications in oncological patients. Lik Sprava. (7-8):94-100.
9) Popiela, T. et al. 2002. Influence of a complementary treatment with oral enzymes on patients with colorectal cancers – an epidemiological retrolective cohort study. Cancer Chemother Pharmacol. 47:55-63.
10) Desser, L. et al. 2001. Oral therapy with proteolytic enzymes decreases excessive TGF-beta levels in human blood. Cancer Chemother Pharmacol. 47:10-5.
11) Lauer, D. et al. 2001. Modulation of growth factor binding properties of alpha2-macroglobulin by enzyme therapy. Cancer Chemother Pharmacol. 47:4-9.

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.