ArticleBiotechnology for biofuels and bioproducts2025
Involvement of the intracellular β-glucosidase BGL1B from Aspergillus niger in the regulation of lignocellulose-degrading enzymes' synthesis.
Article in Biotechnology for biofuels and bioproducts, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Intracellular β-glucosidase regulates cellulase expression and development in Aspergillus nidulans.Applied microbiology and biotechnology · 2026Article
- Multi-omics analysis reveals the carbohydrate-active enzyme repertoire involved in degrading complex arabinoxylans in Penicillium parvum 4-14.Microbial cell factories · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
backgroundAspergillus niger is an important lignocellulose-degrading enzyme-producing strain. Multiple regulatory factors regulate the synthesis of lignocellulose-degrading enzymes in A. niger. We previously found that A. niger possessed an intracellular β-glucosidase BGL1B, and the intracellular localization of BGL1B and its active transglycosylation action prompted us to explore whether BGL1B was involved in the regulation of the synthesis of lignocellulose-degrading enzymes in A. niger.
resultsIn this study, by investigating the production of lignocellulose-degrading enzymes of bgl1B knockout strain (Δbgl1B) and overexpression strain (OE::bgl1B), it was found that BGL1B exhibited a repressive role on the expression of lignocellulose-degrading enzyme genes through carbon catabolite repression (CCR) way. On the other hand, BGL1B's transglycosylation products sophorose and laminaribiose were proved to be able to induce the expression of lignocellulose-degrading enzyme genes, which explained why OE::bgl1B showed the same enhanced enzyme activity and gene expression as Δbgl1B strain compared to the starting strain (WT).
conclusionsThe present study demonstrates that BGL1B plays dual regulatory roles in the regulation of the synthesis of lignocellulose-degrading enzymes in A. niger: the repressive role caused by BGL1B's hydrolysis product glucose and the induction role caused by BGL1B's transglycosylation products sophorose and laminaribiose. This study broadens the understanding of the regulatory network of the synthesis of lignocellulose-degrading enzymes in A. niger. Also, it provides a strategy to create an engineered strain with high production of lignocellulose-degrading enzymes.
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.