ArticleJournal of microbiology (Seoul, Korea)2019
Kinetic characterization of laccase from Bacillus atrophaeus, and its potential in juice clarification in free and immobilized forms.
Article in Journal of microbiology (Seoul, Korea), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed, 27 citations in OpenAlex.
- Recent Advancements for Enhanced Biocatalyst and Biotransformation.Molecular biotechnology · 2026Review
- Immobilized enzymes: exploring its potential in food industry applications.Food science and biotechnology · 2025Review
- Application of Immobilized Enzymes in Juice Clarification.Foods (Basel, Switzerland) · 2023Review
- Laccases as green and versatile biocatalysts: from lab to enzyme market-an overview.Bioresources and bioprocessing · 2021Review
- A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement.Scientific reports · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study, a laccase gene (BaLc) from a lignin degrading bacterium, Bacillus atrophaeus, has been cloned and expressed in Escherichia coli. The optimal catalytic activity of the protein was achieved at 5.5 pH and 35°C temperature, measured by oxidation of ABTS. The K
Indexed as
Identifiers
What OpenQuestion holds
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.