The role of serratiopeptidase in the resolution of inflammation

Inflammation remains a key event during most of the diseases and physiological imbalance. Acute inflammation is an essential physiological event by immune system for a protective measure to remove cause of inflammation and failure of resolution lead to chronic inflammation. Over a period of time, a number of drugs mostly chemical have been deployed to combat acute and chronic inflammation. Recently, enzyme based anti-inflammatory drugs became popular over conventional chemical based drugs. Serratiopeptidase, a proteolytic enzyme from trypsin family, possesses tremendous scope in combating inflammation. Serine protease possesses a higher affinity for cyclooxygenase(COX-Ⅰ and COX-Ⅱ), a key enzyme associated with production of different inflammatory mediators including interleukins(IL),prostaglandins(PGs) and thromboxane(TXs) etc. Currently, arthritis, sinusitis, bronchitis,fibrocystic breast disease, and carpal tunnel syndrome, etc. are the leading inflammatory disorders that affected the entire the globe. In order to conquer inflammation, both acute and chronic world, physician mostly relies on conventional drugs. The most common drugs to combat acute inflammation are Nonsteroidal anti-inflammatory drugs(NSAIDs) alone and or in combination with other drugs. However, during chronic inflammation, NSAIDs are often used with steroidal drugs such as autoimmune disorders. These drugs possess several limitations such as side effects, ADR, etc. In order to overcome these limitations and complications, enzyme based drugs(anti-inflammatory) emerged, and aim for a new high since the last decade. Serine protease, the largest proteolytic family has been reported for several therapeutic applications, including anti-inflammatory. Serratiopeptidase is a leading enzyme which has a very long history in medical as an effective anti-inflammatory drug. Current study emphasizes present scenario and future prospect of serratiopeptidase as an antiinflammatory drug. The study also illustrates a comparative analysis of conventional drugs and enzyme based therapeutic to combat inflammation.

Analytical techniques for serratiopeptidase: A review

A review is presented on different analytical techniques used for qualitative and quantitative analysis of serratiopeptidase, a proteolytic enzyme, which has recently gained importance as an anti-inflammatory agent.Efforts have been made to collate all the relevant references to the extent possible. The review discusses the advantages and disadvantages of the cited analytical techniques, which will help to give insights into the methods used for estimation of serratiopeptidase as such, from clinical isolates and from its dosage forms.The review highlights the basic as well as advanced techniques performed for estimating serratiopeptidase. The techniques illustrated here have been demonstrated to be useful for qualitative and quantitative determination of serratiopeptidase and may find application in analyzing other related proteases.

Screening and molecular characterization of Serratia marcescens VITSD2： A strain producing optimum serratiopeptidase

The current work was attempted to isolate and characterize the serratiopeptidase producing Serratia sp. Among the 10 bacterial isolates 7 strains were identified as Serratia sp. Out of 7 strains one showed potent proteolytic activity and selected for further studies. Based on the morphological, biochemical and molecular characterization, the potent isolate （RH03） was identified as Serratia marcescens （GenBank accession number： KC961637） and the strain was designated as Serratia marcescens VITSD2. The production of serratiopeptidase was carried out in trypticase soya broth and the enzyme was partially purified using ammonium sulfate precipitation and dialysis. The specific activity was determined by casein hydrolysis assay and was found to be 12.00, 21.33, and 25.40 units/rag for crude, precipitated and dialysed samples. The molecular weight of the protease was determined by SDS-PAGE and it was found to be 50 kDa. The antibacterial activity of the produced serratiopeptidase showed moderate activity against Pseudomonas aeruginosa MTCC No. 4676 （12 mm） and Escherichia coli MTCC No. 1588 （15 mm）.

Exploring the bioactive potential of Serriatia marcescens VITAPI （Acc： 1933637） isolated from soil

BACKGROUND： Serratia is one of the most important groups of bacteria which produces proteolytic enzymes effectively and known to possess anti-inflammatory properties. The main focus of the current study was to extract the enzyme serratiopeptidase and pigment prodigiosin from Serratia mascescens. Prodigiosin is a red colored pigment produced by the bacterium Serratia marcescens. It is emerging as a valuable molecule because of its large applications. It has already been proved that pigmented strain of Serratia marcescens is less virulent than non-pigmented strains. Moreover the strain we have obtained is from farm soil which indicates that prodigiosin production can be carded safely using this strain. METHODS： In the present study, the isolate VITASP strain was confirmed by morphological, biochemical and molecular studies. The enzyme and pigment were analyzed for anti-oxidant, anti-inflammatory and cytotoxic properties. RESULTS： The isolate was further confirmed and identified as Serratia marcescens with 99% similarity. The extracted pigment showed potent radical scavenging effect with 86% and the enzyme was found to inhibit 83%, which was significant in comparison to ascorbic acid standard. The in vitro anti-inflammatory effect of pigment in controlled experimental conditions revealed its protection at 88% and the enzyme with 90%. Aspirin was used as the reference drug. The present findings exhibited a concentration dependent inhibition. The cytotoxic bioassay of pigment showed the IC5o value as （50） ~tg/mL with 63% cytotoxicity which was statistically significant compared to positive control. CONCLUSIONS： Therefore, it appears to be an essential remedial and application research. It may turn out to be highly beneficial to mankind in solving many problems associated with human health.

Multi-compartmental transdermal patch for simultaneous delivery of multiple drugs:formulation and evaluation of newly developed novel dosage form

Objective:To evaluate the formulation of multi-compartmental transdermal patches for simultaneous delivery of multiple drugs:aceclofenac and serratiopeptidase.Methods:The patch was prepared by simple solvent casting method using hydroxy propyl methyl celluloseK100Mas matrix forming agent and dimethyl sulphoxide as permeation enhancer.The prepared transdermal patch was evaluated by physiochemical parameters andin-vitro diffusion studies.Results:The multi-compartmental transdermal patch showed sustained drug release over the period of 12 h.Conclusions:Multicompartmental transdermal patches shows better bioavailability,therapeutic efficacy and very economic as compared with other dosage forms.