ArticleAMB Express2021
Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2.
Article in AMB Express, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Investigating bioactive potential of the Serratia sp. CS01 and its pigment for anti-inflammatory, antioxidant and antibacterial action.Scientific reports · 2026Article
- Heterologous expression, purification and functional characterization of recombinant serratiopeptidase from Serratia marcescens AD-W2.World journal of microbiology & biotechnology · 2026Article
- Production, optimization, and purification of serratiopeptidase fromFrontiers in microbiology · 2026Article
- Production of a Recombinant Fibrinolytic Protease from an Isolate of Serratia marcescens from the Amazon Basin.ACS omega · 2025Article
- Increased Proteolytic Activity ofPolish journal of microbiology · 2024Article
- Scale-Up of the Fermentation Process for the Production and Purification of Serratiopeptidase Using Silkworm Pupae as a Substrate.Methods and protocols · 2024Article
- Bioprospecting of serratiopeptidase-producing bacteria from different sources.Frontiers in microbiology · 2024Article
- 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.EFSA journal. European Food Safety Authority · 2024Article
- Serratiopeptidase: An integrated View of Multifaceted Therapeutic Enzyme.Biomolecules · 2022Review
- Correction to: Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2.AMB Express · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serratiopeptidase is a proteolytic enzyme extensively used as an anti-inflammatory and analgesic drug. Present work reports a thermoactive serratiopeptidase from Serratia marcescens AD-W2, a soil isolate from the North-Western Himalayan region of India. The extracellular metalloprotease has been purified by a simple two-step procedure resulting in a specific activity of 20,492 Units/mg protein with 5.28-fold purification. The molecular mass of the metalloprotease, as determined by SDS-PAGE was ~ 51 kDa. The purified serratiopeptidase presented optimum activity at pH 9.0, temperature 50 °C and stability in wide pH and temperature range. Critical temperature of 50 °C confirmed the thermoactivity of the purified serratiopeptidase. The kinetic studies of the purified serratiopeptidase revealed V
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.