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Chymotrypsin

Chymotrypsin is a proteolytic enzyme extracted from beef pancreas that has anti-inflammatory, anti-edematous, fibrinolytic, antioxidant, and anti-infective properties. It is used to help digest proteins, speed healing of traumatic injuries, and reduce pain and inflammation. Trypsin-chymotrypsin combination has emerged as a promising oral treatment to facilitate healing, with faster recovery and better resolution of symptoms than other enzyme preparations. Clinical trials have demonstrated the efficacy and safety of trypsin-chymotrypsin in injuries, surgeries, burns, and other conditions.

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0% found this document useful (0 votes)
60 views4 pages

Chymotrypsin

Chymotrypsin is a proteolytic enzyme extracted from beef pancreas that has anti-inflammatory, anti-edematous, fibrinolytic, antioxidant, and anti-infective properties. It is used to help digest proteins, speed healing of traumatic injuries, and reduce pain and inflammation. Trypsin-chymotrypsin combination has emerged as a promising oral treatment to facilitate healing, with faster recovery and better resolution of symptoms than other enzyme preparations. Clinical trials have demonstrated the efficacy and safety of trypsin-chymotrypsin in injuries, surgeries, burns, and other conditions.

Uploaded by

Roumaissa Derrag
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Introduction

Impaired tissue repair is a common medical problem, affecting millions of people


worldwide. Chronic wounds thus formed are a source of significant morbidity, mortality, and
poor quality of life. They also incur substantial healthcare-related financial burden. Hence,
prompt and effective management of acute tissue injury is necessary to prevent it from
progressing to a chronic wound.

Proteolytic enzymes have been used to facilitate tissue repair since ancient times.

Trypsin: chymotrypsin is an oral proteolytic enzyme preparation which has been in clinical
use since the 1960s. It provides better resolution of inflammatory symptoms and promotes
speedier recovery of acute tissue injury than several of the other existing enzyme preparation.
This paper revisits the role and clinical utility of trypsin: chymotrypsin combination in tissue
repair.
Chymotrypsin utility

Chymotrypsin is a proteolytic enzyme (capable of destroying proteins), extracted from the


pancreas of beef. It’s indicated in:

 Ophthalmology to reduce trauma to the eye during lens operations.


 It’s biological activities as an anti-inflammatory, anti-edematous, fibrinolytic,
antioxidant, and anti-infective agent.
 Chymotrypsin enzymes are primarily used by people who could use a little support
with digesting and absorbing proteins.
 Also used in clinical settings to help speed up the repair of traumatic, surgical, and
orthopedic injuries.[04]

These properties help in resolving sings and symptoms of inflammation due to tissue injury
and facilitate the repair process. It also demonstrates analgesic effects and reduces the pain
associated with healing.

Chymotrypsin is prescribed orally, injected or topically.[05]


Conclusion
Owing to anti-inflammatory, anti-edematous, fibrinolytic, anti-infective, and analgesic
effects, trypsin: chymotrypsin oral combination has emerged as a promising treatment to
facilitate healing of traumatic injuries. It promotes speedier recovery and better resolution of
inflammatory signs and symptoms due to tissue injury than several of the other existing
enzyme preparation.

It also demonstrates analgesic effects and reduces pain associated with healing. The efficacy
and safety of trypsin: chymotrypsin in accidental injuries, surgical and orthopedic injuries,
burns, and sciatica has been corroborated by a substantial and largely consistent body of
evidence from clinical trials.
Reference

[04]: Hartley,(B).(S). Proteolytic enzymes. Annual review of Biochemistry (1960).Vol.29, no


1, p. 45-72.

[05]: Goel.(VK), Sengupta.(B). The use of chymoral tables in accident and casualty
departments. Br Assoc Sports Med J.(1973). Vol 7, no (1&2), p. 67-69.

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