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Production, purification, characterization, immobilization, and application of Serrapeptase: a review

  • Review
  • Published:
Frontiers in Biology

Abstract

Background

Serrapeptase is a proteolytic enzyme with many favorable biological properties like anti-inflammatory, analgesic, anti-bacterial, fibrinolytic properties and hence, is widely used in clinical practice for the treatment of many diseases. Although Serrapeptase is widely used, there are very few published papers and the information available about the enzyme is very meagre. Hence this review article compiles all the information about this important enzyme Serrapeptase.

Methods

A literature search against various databases and search engines like PubMed, SpringerLink, Scopus etc. was performed.

Results

We gathered and highlight all the published information regarding the molecular aspects, properties, sources, production, purification, detection, optimizing yield, immobilization, clinical studies, pharmacology, interaction studies, formulation, dosage and safety of the enzyme Serrapeptase.

Conclusion

Serrapeptase is used in many clinical studies against various diseases for its anti-inflammatory, fibrinolytic and analgesic effects. There is insufficient data regarding the safety of the enzyme as a health supplement. Data about the antiatherosclerotic activity, safety, tolerability, efficacy and mechanism of action of the Serrapeptase are still required.

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Acknowledgements

The authors would like to thank SRM University, Chennai, India for supporting and performing the study. SG is obliged to the management of SRM for partial completion of masters in Genetic Engineering.

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  1. Department of Genetic Engineering, School of Bioengineering, SRM University, Kattankulathur, Tamil Nadu, India

    Selvarajan Ethiraj & Shreya Gopinath

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  1. Selvarajan Ethiraj
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  2. Shreya Gopinath
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Correspondence to Selvarajan Ethiraj.

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Ethiraj, S., Gopinath, S. Production, purification, characterization, immobilization, and application of Serrapeptase: a review. Front. Biol. 12, 333–348 (2017). https://doi.org/10.1007/s11515-017-1461-3

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  • DOI: https://doi.org/10.1007/s11515-017-1461-3

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