ArticleJournal, genetic engineering & biotechnology2019
Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source.
Article in Journal, genetic engineering & biotechnology, 2019. 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, 27 citations in OpenAlex.
- Production, optimization, and purification of serratiopeptidase fromFrontiers in microbiology · 2026Article
- Article
- Network pharmacology and molecular docking: combined computational approaches to explore the antihypertensive potential of Fabaceae species.Bioresources and bioprocessing · 2024Article
- Scale-Up of the Fermentation Process for the Production and Purification of Serratiopeptidase Using Silkworm Pupae as a Substrate.Methods and protocols · 2024Article
- Novel marine metalloprotease-new approaches for inhibition of biofilm formation of Stenotrophomonas maltophilia.Applied microbiology and biotechnology · 2023Article
- Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2.AMB Express · 2021Article
- Serratiopeptidase: Insights into the therapeutic applications.Biotechnology reports (Amsterdam, Netherlands) · 2020Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSerratiopeptidase is an alkaline metalloendopeptidase, which acquired wide significance because of its therapeutic applications. The present study was undertaken for purification, characterization, and structural elucidation of serratiopeptidase produced from Streptomyces hydrogenans var. MGS13.
resultThe crude enzyme was purified by precipitating with ammonium sulfate, dialysis, and Sephadex gel filtration, resulting in 34% recovery with a 12% purification fold. The purified enzyme S.AMP13 was spotted as a single clear hydrolytic band on casein zymogram and whose molecular weight was found to be 32 kDa by SDS-PAGE. The inhibitor and stability studies revealed that this enzyme is metalloprotease, thermostable, and alkaline in nature. The maximum serratiopeptidase activity was observed at 37 °C and pH 9.0. The partial amino acid sequence of the purified enzyme S.AMP13 by LC-MS/MS analysis shows the closest sequence similarities with previously reported alkaline metalloendopeptidases. The amino acid sequence alignment of S.AMP13 shared a conserved C-terminus region with peptidase-M10 serralysin superfamily at amino acid positions 128-147, i.e., ANLSTRATDTVYGFNSTAGR revealed that this enzyme is a serralysin-like protease. The kinetic studies of the purified enzyme revealed a K
conclusionInhibitor, stability, electrophoretic, and bioinformatic studies suggested that the purified enzyme obtained from S. hydrogenans var. MGS13 is a serralysin-like protease.
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