ArticleBiotechnology letters2025
Improvement in lignin peroxidase oxidative stability via surface display by Bacillus subtilis.
Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lignin peroxidase (LiP) is a key enzyme involved in lignin degradation. However, the production of natural LiP is limited by the low enzyme-producing capacity of native fungal hosts and the poor stability of the enzyme, hindering its industrialization. To overcome these limitations, we prepared an immobilized enzyme by fusing the LiP gene with the Bacillus subtilis (B. subtilis) spore coat protein CotB and displaying it on the bacterial surface. This approach aims to improve enzymatic stability and industrial applicability. Enzymatic characterization showed that the immobilized LiP exhibited optimal activity at 50 °C and pH 5.0, representing a 10 °C increase over the optimal temperature (40 °C) and a lower pH optimum compared to free LiP (pH 6.0). Under extreme conditions (70 °C, 6 h), the free enzyme retained less than 10% residual activity, whereas CotB-LiP maintained 42.7% ± 1.37% activity. After 1 h incubation in 1 mM H
Indexed as
Identifiers
40762737What 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.