ArticleFrontiers in microbiology2024
Bioprospecting of serratiopeptidase-producing bacteria from different sources.
Article in Frontiers in microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Exploring the plant growth-promoting potential of cormobacteria of saffron grown in a non-traditional cultivation region during two growth stages.Folia microbiologica · 2026Article
- Investigating bioactive potential of the Serratia sp. CS01 and its pigment for anti-inflammatory, antioxidant and antibacterial action.Scientific reports · 2026Article
- Bioprospecting of Aerobic Bacteria with Proteolytic Potential Isolated from Animal and Water Sources in the Three Regions of Mainland Ecuador.International journal of molecular sciences · 2026Article
- Production, optimization, and purification of serratiopeptidase fromFrontiers in microbiology · 2026Article
- Experimental analysis and genome mining for functional validation of genes associated with anti-inflammatory, antioxidant, and antibacterial activities inFrontiers in pharmacology · 2026Article
- Statistical optimization of process variables for enhanced serratiopeptidase production from soil Serratia marcescens VS56.Scientific reports · 2025Article
- Enzyme-Based Anti-Inflammatory Therapeutics for Inflammatory Diseases.Pharmaceutics · 2025Review
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Authors and funding
2 authors.
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Abstract
Anti-inflammatory enzymes have wide applications in the pharmaceutical industry. The objective of this study was to find new and efficient strains for the commercial production of serratiopeptidase enzyme. Vast number of samples were processed for the isolation of potent strains. The experimental treatment includes processing of twenty soil samples, silkworm gut, and sugarcane stem. The total protein and protease activity was estimated by Lowry's method and casein hydrolysis. The HRBC stabilization assay was performed for finding the anti-inflammatory potential of all strains. The serratiopeptidase production was confirmed by HPLC with the standard. Molecular characterization of selected potent strains was done by 16S rDNA and confirmed the taxonomy. The one step rapid purification of serratiopeptidase was performed by Ultra three phase partitioning method. The clot lysis potential of the
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