{
      "number": 3,
      "subjects": [
        "QR"
      ],
      "eprintid": 3465,
      "date": "2026-02-24",
      "userid": 2,
      "documents": [
          {
            "placement": 1,
            "eprintid": 3465,
            "files": [
                {
                  "hash_type": "MD5",
                  "mtime": "2026-07-10 01:40:14",
                  "datasetid": "document",
                  "fileid": 29206,
                  "objectid": 5755,
                  "uri": "http:\/\/crdd.osdd.net\/open\/id\/file\/29206",
                  "mime_type": "text\/x-bibtex",
                  "hash": "70b9841fccee06b9c5575b1318f7947c",
                  "filesize": 2743,
                  "filename": "references.bib"
                }
            ],
            "rev_number": 2,
            "uri": "http:\/\/crdd.osdd.net\/open\/id\/document\/5755",
            "main": "references.bib",
            "mime_type": "text\/x-bibtex",
            "docid": 5755,
            "format": "text\/html",
            "security": "public",
            "pos": 1
          }
      ],
      "official_url": "https:\/\/link.springer.com\/article\/10.1007\/s11274-026-04795-3",
      "rev_number": 7,
      "creators": [
        {
          "name": {
            "lineage": null,
            "given": "Devtulya",
            "honourific": null,
            "family": "Chander"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Diksha",
            "honourific": null,
            "family": "Koul"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Shubham",
            "honourific": null,
            "family": "Singh"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Ravi S.",
            "honourific": null,
            "family": "Manhas"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Diljeet",
            "honourific": null,
            "family": "Kumar"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Sanket",
            "honourific": null,
            "family": "Shukla"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Ravi P. N.",
            "honourific": null,
            "family": "Mishra"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Zabeer",
            "honourific": null,
            "family": "Ahmed"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Asha",
            "honourific": null,
            "family": "Chaubey"
          }
        }
      ],
      "dir": "disk0\/00\/00\/34\/65",
      "keywords": "<italic>E.coli<\/italic> K12; serratiopeptidase; Protein refolding; Tangential flow filtration; Anti-inflammatory activity",
      "lastmod": "2026-07-10 01:43:41",
      "ispublished": "pub",
      "publisher": "SPRINGER",
      "metadata_visibility": "show",
      "date_type": "published",
      "eprint_status": "archive",
      "status_changed": "2026-07-10 01:43:41",
      "volume": 42,
      "datestamp": "2026-07-10 01:43:41",
      "uri": "http:\/\/crdd.osdd.net\/open\/id\/eprint\/3465",
      "note": "Copyright of this data belongs to WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY",
      "refereed": "TRUE",
      "contact_email": "kps.sengar@csir.res.in",
      "publication": "WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY",
      "abstract": "Serratiopeptidase, a proteolytic enzyme with therapeutic applications, is traditionally produced from the bacterium Serratia marcescens. Recombinant production of serratiopeptidase in Escherichia coli offers a safer alternative to the biosafety concerns of the producer. Present study involves cloning and heterologous expression of thermoactive serratiopeptidase gene from S. marcescens AD-W2 in E. coli K12 in pET28a plasmid. Optimized expression conditions i.e. 37 degrees C, OD600 5, 5% L-rhamnose, 5mM IPTG, and 50% dissolved oxygen led to the final yield of 190 mg\/g serratiopeptidase (4747 mg protein\/L within 9 h in a bioreactor. Purification and refolding of recombinant serratiopeptidase was performed in a single step using Tangential Flow Filtration (TFF) and diafiltration process. The purified recombinant serratiopeptidase exhibited specific activity of 1800 Units\/mg protein, with an optimal activity at pH 9.0 and temperature 50 degrees C. The value of kinetic constant Km was calculated as 1.38 mg\/mL for casein. The recombinant serratiopeptidase demonstrated comparable anti-inflammatory activity to the commercially available serratiopeptidase, inhibiting nitric oxide release and pro-inflammatory cytokine production in LPS-stimulated murine macrophage cell line RAW 264.7. The study reveals that the recombinant serratiopeptidase produced in E. coli K12 holds promising source of safe and effective anti-inflammatory agent.",
      "type": "article",
      "title": "Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2",
      "place_of_pub": "VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS"
    }