VitalSerra P20- Serratiopeptidase [2,000 to 2,600 IU/ mg] powder
- VitalSerra; Serratiopeptidase; Serralysin; Serratia-protease; Serrapeptidase; Serrapeptase
- CAS Number: 37312-62-2
- EC Number: 253-457-5
VitalSerra P20- Serratiopeptidase [2,000 to 2,600 IU/ mg] powder
BackgroundSerratiopeptidase is a proteolytic (protein breakdown) enzyme. Serratiopeptidase, also known as serralysin, Serratia-protease, serrapeptidase and serrapeptase, is a proteolytic enzyme with therapeutic applications. Traditionally, serratiopeptidase was used for its anti-inflammatory and analgesic properties, and much of modern research has supported its use in these areas (Tiwari, 2017). VitalSerra is produced by a fermentation process using enterobacterium of Serratia species.
At Present we have the following variants of VitalSerraVitalSerra P20 - Serratiopeptidase [2,000 to 2,600 IU/ mg] powder
VitalSerra G20 - Serratiopeptidase [2,000 to 2,600 IU/ mg] granular Powder
VitalSerra E20 - Serratiopeptidase [2,000 to 2,600 IU/ mg] granular powder – enteric coated
StructureSerratiopeptidase is a zinc containing metalloprotease of molecular weight 45–60 kDa, comprised of 470 amino acids. The zinc molecule helps catalyse its enzymatic activity. The enzyme has an EC number 188.8.131.52 and belongs to the group Serralysin.
Health BenefitsSerratiopeptidase is commonly used after surgeries, in orthopaedics, gynaecology, otolaryngology and dentistry due to its anti-inflammatory, pain relieving properties (Bhagat et al., 2013). However, serratiopeptidase’s actions are not limited to this.
Anti-inflammatoryInflammation is a result of the immune system rapidly responding to any foreign or unwanted changes in bodily tissues which leads to the recruitment of immune cells and multiple other inflammatory mediators (Tiwari, 2017).
Serratiopeptidase acts as an anti-inflammatory through multiple mechanisms. One such way is by decreasing the amount of fluid in tissues when swelling occurs, which it does by thinning the fluid and facilitating the drainage of it (Bhagat et al., 2013). In addition, serratiopeptidase dissolves dead tissue surrounding an injured area, subsequently accelerating the healing (Jadhav et al., 2020).
A third mechanism by which it reduces inflammation is by modifying cell-surface adhesion molecules that act as guides for inflammatory cells to their target site of inflammation. Due to serratiopeptidase’s influence on these adhesion molecules, it may be beneficial for the treatment of autoimmune diseases such as arthritis as these molecules play an important role in the development of these diseases (Klein & Kullich, 2000).
Inflammation can be both acute and chronic. Acute inflammation is a protective mechanism against injury or infection however, chronic inflammation is a result of the failure of acute inflammation resolution. Inflammatory disorders include arthritis, bronchitis and carpal tunnel syndrome. Acute inflammation is generally treated with non-steroidal anti-inflammatory drugs (NSAIDs), whereas steroidal drugs are prescribed, and used in conjunction with NSAIDs to combat chronic inflammation. Serratiopeptidase has shown to be beneficial as an anti-inflammatory treatment both alone, as well as when used in conjunction with NSAIDs such as aspirin in order to reduce inflammation (Viswanatha Swamy & Patil, 2008).
Acutely, serratiopeptidase has been successfully used as an anti-inflammatory agent following from minor surgical procedures such as the removal of wisdom teeth as well as decreasing pain and improving movement of the jaw (Sivaramakrishnan & Sridharan, 2017). As well as its effectiveness, serratiopeptidase has gained popularity due to its safety profile, proving a safe alternative in cases of intolerance or adverse side effects to other medications.
Pain ReliefSerratiopeptidase has also been shown to reduce pain by inhibiting pain-inducing compounds from inflamed tissues. These compounds are amines such as bradykinin (Mazzone et al., 1990). Bradykinin mediates inflammation by causing vasodilation, by increasing vascular permeability, and by stimulating the synthesis of prostaglandins. Bradykinin causes pain by directly stimulating primary sensory neurons and provoking the release of substance P, neurokinin, and calcitonin gene-related peptide (Enna & Bylund, 2008).
Association with AntibioticsAntibiotics are often overused in today’s society, decreasing their effectiveness (Davies & Davies, 2010). Therefore, an ingredient such as serratiopeptidase which has been shown to increase the effectiveness of antibiotics has great importance.
There is a physiological mechanism in which bacteria can join together to form a protective barrier around their group, this barrier then acts as a shield against antibiotics which allows bacteria to grow rapidly and cause infection (Lacout et al., 2018). Serratiopeptidase has been shown to inhibit the formation of this barrier, therefore increasing the effectiveness of antibiotics.
Research suggests that the combination of serratiopeptidase and antibiotics has been found to be more effective than antibiotics alone, and importantly, the combination of the two has been shown to be effective in treating infections that have become resistant to antibiotics (Selan et al., 2015; Selan et al., 2017).
Artery HealthThere has been a small amount of research to indicate that serratiopeptidase may help dissolve blood clots. When plaque builds up inside arteries, this is known as atherosclerosis, this can eventually lead to the development of blood clots which can cause strokes or heart attacks. Serratiopeptidase may act by breaking down fibrin and other dead or damaged tissue whilst not harming living tissue (Bhagat et al., 2013). It is important to note, that due to the nature of this ingredient, caution should be given around its use concurrently with blood thinning or clotting medications.
- Bhagat, S., Agarwal, M. and Roy, V., 2013. Serratiopeptidase: A systematic review of the existing evidence. International Journal of Surgery, 11(3), pp.209-217.
- Davies, J. and Davies, D., 2010. Origins and Evolution of Antibiotic Resistance. Microbiology and Molecular Biology Reviews, 74(3), pp.417-433.
- Enna, S. and Bylund, D., 2008. XPharm. Amsterdam: Elsevier.
- Jadhav, S., Shah, N., Rathi, A., Rathi, V. and Rathi, A., 2020. Serratiopeptidase: Insights into the therapeutic applications. Biotechnology Reports, 28, p.e00544.
- Klein, G. and Kullich, W., 2000. Short-Term Treatment of Painful Osteoarthritis of the Knee with Oral Enzymes. Clinical Drug Investigation, 19(1), pp.15-23.
- Lacout, A., Dacher, V., El Hajjam, M., Marcy, P. and Perronne, C., 2018. Biofilms busters to improve the detection of Borrelia using PCR. Medical Hypotheses, 112, pp.4-6.
- Mazzone, A., Catalani, M., Costanzo, M., Drusian, A., Mandoli, A., Russo, S., Guarini, E. and Vesperini, G., 1990. Evaluation of Serratia Peptidase in Acute or Chronic Inflammation of Otorhinolaryngology Pathology: A Multicentre, Double-Blind, Randomized Trial versus Placebo. Journal of International Medical Research, 18(5), pp.379-388.
- Selan, L., Papa, R., Ermocida, A., Cellini, A., Ettorre, E., Vrenna, G., Campoccia, D., Montanaro, L., Arciola, C. and Artini, M., 2017. Serratiopeptidase reduces the invasion of osteoblasts by Staphylococcus aureus. International Journal of Immunopathology and Pharmacology, 30(4), pp.423-428.
- Selan, L., Papa, R., Tilotta, M., Vrenna, G., Carpentieri, A., Amoresano, A., Pucci, P. and Artini, M., 2015. Serratiopeptidase: a well-known metalloprotease with a new non-proteolytic activity against S. aureus biofilm. BMC Microbiology, 15(1).
- Sivaramakrishnan, G. and Sridharan, K., 2017. Role of Serratiopeptidase After Surgical Removal of Impacted Molar: A Systematic Review and Meta-analysis. Journal of Maxillofacial and Oral Surgery, 17(2), pp.122-128.
- Tiwari, M., 2017. The role of serratiopeptidase in the resolution of inflammation. Asian Journal of Pharmaceutical Sciences, 12(3), pp.209-215.
- Viswanatha Swamy, A. and Patil, P., 2008. Effect of some clinically used proteolytic enzymes on inflammation in rats. Indian Journal of Pharmaceutical Sciences, 70(1), p.114.
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