ArticleEnzyme research2016
Highly Active and Stable Large Catalase Isolated from a Hydrocarbon Degrading Aspergillus terreus MTCC 6324.
Article in Enzyme research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Heterologous expression of a heme-dependent catalase from Avicennia marina confers multi-stress tolerance in Escherichia coli for biotechnological applications.Scientific reports · 2026Article
- The Richness and Diversity of Catalases in Bacteria.Frontiers in microbiology · 2021Article
- First ecotoxicological characterization of paraffin microparticles: a biomarker approach in a marine suspension-feeder, Mytilus sp.Environmental science and pollution research international · 2020Article
- Biochemical Characteristics of Microbial Enzymes and Their Significance from Industrial Perspectives.Molecular biotechnology · 2019Review
- Article
- Oxidative Stress Response Tips the Balance in Aspergillus terreus Amphotericin B Resistance.Antimicrobial agents and chemotherapy · 2017Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A hydrocarbon degrading Aspergillus terreus MTCC 6324 produces a high level of extremely active and stable cellular large catalase (CAT) during growth on n-hexadecane to combat the oxidative stress caused by the hydrocarbon degrading metabolic machinery inside the cell. A 160-fold purification with specific activity of around 66 × 10(5) U mg(-1) protein was achieved. The native protein molecular mass was 368 ± 5 kDa with subunit molecular mass of nearly 90 kDa, which indicates that the native CAT protein is a homotetramer. The isoelectric pH (pI) of the purified CAT was 4.2. BLAST aligned peptide mass fragments of CAT protein showed its highest similarity with the catalase B protein from other fungal sources. CAT was active in a broad range of pH 4 to 12 and temperature 25°C to 90°C. The catalytic efficiency (K cat/K m ) of 4.7 × 10(8) M(-1) s(-1) within the studied substrate range and alkaline pH stability (half-life, t 1/2 at pH 12~15 months) of CAT are considerably higher than most of the extensively studied catalases from different sources. The storage stability (t 1/2) of CAT at physiological pH 7.5 and 4°C was nearly 30 months. The haem was identified as haem b by electrospray ionization tandem mass spectroscopy (ESI-MS/MS).
Identifiers
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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.