Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2

Chander, Devtulya; Khosla, Jasmine Kour; Koul, Diksha; Hossain, Md Mehedi; Dar, Mohd Jamal; Chaubey, Asha

doi:10.1186/s13568-021-01215-7

Cited by 9 publications

(8 citation statements)

References 26 publications

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“…Serratia zymography pattern is poorly defined, nonetheless obtained results with HU1848 and Db10 resemble zymogram data of pioneer work in S. marcescens strain BG ( Lyerly and Kreger 1979 ). In contrast, a unique proteolytic zone (similar to SmUNAM836) was also described in the supernatant of the environmental strain AD-W2 ( Chander et al 2021 ).…”

Section: Resultsmentioning

confidence: 98%

Increased Proteolytic Activity of Serratia marcescens Clinical Isolate HU1848 Is Associated with Higher eepR Expression

De Anda-Mora,

Tavares-Carreón,

Alvarez

et al. 2024

Polish Journal of Microbiology

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Serratia marcescens is a global opportunistic pathogen. In vitro cytotoxicity of this bacterium is mainly related to metalloprotease serralysin (PrtS) activity. Proteolytic capability varies among the different isolates. Here, we characterized protease production and transcriptional regulators at 37°C of two S. marcescens isolates from bronchial expectorations, HU1848 and SmUNAM836. As a reference strain the insect pathogen S. marcescens Db10 was included. Zymography of supernatant cultures revealed a single (SmUNAM836) or double proteolytic zones (HU1848 and Db10). Mass spectrometry confirmed the identity of PrtS and the serralysin-like protease SlpB from supernatant samples. Elevated proteolytic activity and prtS expression were evidenced in the HU1848 strain through azocasein degradation and qRT-PCR, respectively. Evaluation of transcriptional regulators revealed higher eepR expression in HU1848, whereas cpxR and hexS transcriptional levels were similar between studied strains. Higher eepR expression in HU1848 was further confirmed through an in vivo transcriptional assay. Moreover, two putative CpxR binding motifs were identified within the eepR regulatory region. EMSA validated the interaction of CpxR with both motifs. The evaluation of eepR transcription in a cpxR deletion strain indicated that CpxR negatively regulates eepR. Sequence conservation suggests that regulation of eepR by CpxR is common along S. marcescens species. Overall, our data incorporates CpxR to the complex regulatory mechanisms governing eepR expression and associates the increased proteolytic activity of the HU1848 strain with higher eepR transcription. Based on the global impact of EepR in secondary metabolites production, our work contributes to understanding virulence factors variances across S. marcescens isolates.

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Section: Resultsmentioning

confidence: 98%

Increased Proteolytic Activity of Serratia marcescens Clinical Isolate HU1848 Is Associated with Higher eepR Expression

De Anda-Mora,

Tavares-Carreón,

Alvarez

et al. 2024

Polish Journal of Microbiology

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“…S. marcescens is a ubiquitous bacterium displaying a high genetic plasticity that allows it to adapt and persist in multiple niches including soil, water and plants. It has been recently described for the production of serratiopeptidase, a proteolytic enzyme extensively used as an anti‐inflammatory and analgesic drug (Chander et al., 2021 ). Prodigiosin, a red pigment produced by this species, demonstrated toxigenic effects on chick embryos and antimicrobial activity (Kalesperis et al., 1975 ).…”

Section: Assessmentmentioning

confidence: 99%

Update of the list of qualified presumption of safety (QPS) recommended microbiological agents intentionally added to food or feed as notified to EFSA 19: Suitability of taxonomic units notified to EFSA until September 2023

Koutsoumanis,

Allende,

Alvarez‐Ordóñez

et al. 2024

EFS2

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The qualified presumption of safety (QPS) process was developed to provide a safety assessment approach for microorganisms intended for use in food or feed chains. The QPS approach is based on an assessment of published data for each taxonomic unit (TU), with respect to its taxonomic identity, the body of relevant knowledge and safety concerns. Safety concerns identified for a TU are, where possible, confirmed at the species/strain or product level and reflected by ‘qualifications’. In the period covered by this Statement, no new information was found that would change the status of previously recommended QPS TUs. Of 71 microorganisms notified to EFSA between April and September 2023 (30 as feed additives, 22 as food enzymes or additives, 7 as novel foods and 12 from plant protection products [PPP]), 61 were not evaluated because: 26 were filamentous fungi, 1 was Enterococcus faecium, 5 were Escherichia coli, 1 was a bacteriophage (all excluded from the QPS evaluation) and 28 were TUs that already have a QPS status. The other 10 notifications belonged to 9 TUs which were evaluated for a possible QPS status: Ensifer adhaerens and Heyndrickxia faecalis did not get the QPS recommendation due to the limited body of knowledge about their occurrence in the food and/or feed chains and Burkholderia ubonensis also due to its ability to generate biologically active compounds with antimicrobial activity; Klebsiella pneumoniae, Serratia marcescens and Pseudomonas putida due to safety concerns. K. pneumoniae is excluded from future QPS evaluations. Chlamydomonas reinhardtii is recommended for QPS status with the qualification ‘for production purposes only’; Clostridium tyrobutyricum is recommended for QPS status with the qualification ‘absence of genetic determinants for toxigenic activity’; Candida oleophila has been added as a synonym of Yarrowia lipolytica. The Panel clarifies the extension of the QPS status for genetically modified strains.

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“…Industries have always given priority to such stable organisms. The study on thermoactive serratiopeptidase [ 44 ] from the soil isolate Serratia marcescens AD-W2 from India’s North-Western Himalayan area showed a specific activity of 20,492 units/mg protein with 5.28-fold purification. The molecular weight of the metalloprotease was approximately 51 kDa.…”

Section: Enzyme Productionmentioning

confidence: 99%

“…The molecular weight of the metalloprotease was approximately 51 kDa. At pH 9.0 and 50 °C, the purified serratiopeptidase showed maximum activity, in addition to stability over a wide range of pH values and temperatures [ 44 ]. The thermostability of the enzyme was considered to be one of the most significant properties for the large-scale industrial production.…”

Section: Enzyme Productionmentioning

confidence: 99%

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Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme

Nair

Devi

2022

Biomolecules

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Microbial products have been used for the treatment of different diseases for many centuries. The serratiopeptidase enzyme provides a new hope for COVID-19-infected patients. Nowadays, anti-inflammatory drugs are easy to obtain at minimal expenditure from microbial sources. Serratia sp. is identified as one of the most efficient bacteria produced from serratiopeptidase. Screening for new and efficient bacterial strains from different sources has been of interest in recent years. Serratiopeptidase remains the most well-known anti-inflammatory drug of choice. Serratiopeptidase is a cheaper and safer anti-inflammatory drug alternative to NSAIDs. The multifaceted properties of serratiopeptidase may lead towards arthritis, diabetes, cancer and thrombolytic treatments. Existing serratiopeptidase treatments in combination with antibiotics are popular in the treatment of postoperative swelling. Although an exclusive number of serratiopeptidase-producing strains have been derived, there is an urge for new recombinant strains to enhance the production of the enzyme. This review explores the properties of serratiopeptidase, different therapeutic aspects, industrial production, and various analytical techniques used in enzyme recovery. In addition, the review highlights the therapeutic and clinical aspects of the serratiopeptidase enzyme to combat COVID-19-induced respiratory syndrome.

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Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2

Cited by 9 publications

References 26 publications

Increased Proteolytic Activity of Serratia marcescens Clinical Isolate HU1848 Is Associated with Higher eepR Expression

Increased Proteolytic Activity of Serratia marcescens Clinical Isolate HU1848 Is Associated with Higher eepR Expression

Update of the list of qualified presumption of safety (QPS) recommended microbiological agents intentionally added to food or feed as notified to EFSA 19: Suitability of taxonomic units notified to EFSA until September 2023

Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme

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