Evidence map›Paper›PMID 40057735›Full record

ArticleMicrobial cell factories2025

Production and characterization of a promising microbial-derived lipase enzyme targeting BCL-2 gene expression in hepatocellular carcinoma.

Amal M Abo-Kamer, Ahmed A Abdelaziz, Esraa S Elkotb, Lamiaa A Al-Madboly

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Article in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

4 authors.

Amal M Abo-KamerDepartment of Microbiology and Immunology, Faculty of Pharmacy, Tanta University, Tanta, Egypt.
Ahmed A AbdelazizDepartment of Microbiology and Immunology, Faculty of Pharmacy, Tanta University, Tanta, Egypt.
Esraa S ElkotbDepartment of Microbiology and Immunology, Faculty of Pharmacy, Tanta University, Tanta, Egypt.
Lamiaa A Al-MadbolyDepartment of Microbiology and Immunology, Faculty of Pharmacy, Tanta University, Tanta, Egypt. lamia.youssif@pharm.tanta.edu.eg.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

context and goalThis study aimed to isolate and optimize a high-yield lipase-producing Pseudomonas aeruginosa strain from biological samples, enhance enzyme production through random mutagenesis, and evaluate its potential anticancer activity. Fifty-one biological samples (blood, urine, sputum, wound pus) were screened, and three isolates demonstrated significant lipase activity. The isolate with the highest activity, identified as P. aeruginosa (GenBank accession number PP436388), was subjected to ethidium bromide-induced mutagenesis, resulting in a two-fold increase in lipase activity (312 U/ml). Lipase production was optimized using submerged fermentation, with critical factors identified statistically as Tween 80, peptone, and substrate concentration. The enzyme was purified via ammonium sulfate precipitation and Sephadex G-100 chromatography, and its molecular weight (53 kDa) was confirmed by SDS-PAGE.

findingsOptimal conditions for enzyme production included a pH of 9, temperature of 20 °C, and a 24-h incubation period. The partially purified enzyme exhibited high stability at pH values up to 10 and storage temperatures of 4 °C. Anticancer activity was evaluated using the MTT assay, revealing an IC

Indexed as

Antineoplastic AgentsCarcinoma, HepatocellularLipaseLiver NeoplasmsProto-Oncogene Proteins c-bcl-2Pseudomonas aeruginosaAnimalsChlorocebus aethiopsHep G2 CellsHumansVero CellsAntineoplastic AgentsLipaseProto-Oncogene Proteins c-bcl-2AnticancerBiological samplesHepatocellular carcinoma (HepG-2)LipaseMutant lipolytic activityOptimizationScreening

Identifiers

PMID40057735
PMCPMC11890718

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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.