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primary topic: Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2

Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2
type: AcademicArticle
type: Article
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.
date: 2026-02-24
volume: 42
issue: 3
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
has document: Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2 (HTML)
subject: QR Microbiology

Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2 (HTML)
type: Document
has file: references.bib
has part: references.bib

SPRINGER
type: Organization

WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
type: Collection

Ravi P. N. Mishra
type: Person
given name: Ravi P. N.
family name: Mishra

Ravi S. Manhas
type: Person
given name: Ravi S.
family name: Manhas

Zabeer Ahmed
type: Person
given name: Zabeer
family name: Ahmed

Diljeet Kumar
type: Person
given name: Diljeet
family name: Kumar

Shubham Singh
type: Person
given name: Shubham
family name: Singh

Asha Chaubey
type: Person
given name: Asha
family name: Chaubey

Sanket Shukla
type: Person
given name: Sanket
family name: Shukla

Diksha Koul
type: Person
given name: Diksha
family name: Koul

Devtulya Chander
type: Person
given name: Devtulya
family name: Chander

HTML Summary of #3465 Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2
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primary topic: Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2

QR Microbiology
type: Concept