ArticleMicrobial cell factories2026
Pleurotus ostreatus L-asparaginase's use in food safety and biotechnology: from processing assistance to bioactive agent.
Article in Microbial cell factories, 2026. 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
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND AND
aimL-ASNase has attracted attention in many biomedical and food safety applications. Therefore, this study was designed to identify a novel and promising candidate for the sustainable biosynthesis of extracellular L-ASNase from P. ostreatus AUMC 16015 grown on various agricultural substrates under solid-state fermentation (SSF). Also, the enzyme's wide-ranging bioactivities were examined, involving its antioxidant, anti-inflammatory, and antitumor properties, while evaluating its potential applications in food processing.
resultsOptimal P. ostreatus AUMC 16015 L-ASNase production was 56.47 U/mL, which was attained under SSF conditions where the enzyme yield increased by 2.46-fold compared to pre-optimization conditions. Enzyme high purity was validated by a single distinct band at approximately 48 kDa on both SDS-PAGE and native PAGE analyses. The enzyme demonstrated high substrate specificity (K
conclusionThe biochemical activity of the purified L-ASNase suggested potential biomedical and food applications. This study is a trial for cost-effective enzyme production and supports a circular bioeconomy by converting waste into useful bioproducts. Future work should focus on scaling up production and testing its effects in living organisms to unlock this enzyme's full commercial and medical potential.
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.