ArticleApplied and environmental microbiology2023
Loosenin-Like Proteins from
Article in Applied and environmental microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Catalysis does not explain expansin-mediated wall creep: Distinguishing catalytic ERPs from creep-active expansins.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Functional characterization of a dockerin-containing expansin-like protein from the anaerobic fungus Neocallimastix californiae.Biotechnology for biofuels and bioproducts · 2026Article
- Uncovering Sequence and Structural Characteristics of Fungal Expansin-Related Proteins With Potential to Drive Substrate Targeting.Proteins · 2026Article
- A single-domain expansin-like protein fromProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Selected cell wall-associated components in plant defense responses against microbial pathogens.Frontiers in plant science · 2026Review
- Mining expansin-like proteins from rumen microbiota and functional characterization of two anaerobic fungal expansin-like proteins.Journal of animal science and biotechnology · 2025Article
- Carbohydrate-binding domain CBM63 of microbial expansin-like BsEXLX1 facilitates the adsorption of expansin-related proteins to hemicelluloses in plant secondary cell walls.Biotechnology for biofuels and bioproducts · 2025Article
- Expansins in Salt and Drought Stress Adaptation: From Genome-Wide Identification to Functional Characterisation in Crops.Plants (Basel, Switzerland) · 2025Review
- SANS investigation of fungal loosenins reveals substrate-dependent impacts of protein action on the inter-microfibril arrangement of cellulosic substrates.Biotechnology for biofuels and bioproducts · 2025Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microbial expansin-related proteins are ubiquitous across bacterial and fungal organisms and reportedly play a role in the modification and deconstruction of cell wall polysaccharides, including lignocellulose. So far, very few microbial expansin-related proteins, including loosenins and loosenin-like (LOOL) proteins, have been functionally characterized. Herein, four LOOLs encoded by Phanerochaete carnosa and belonging to different subfamilies (i.e., PcaLOOL7 and PcaLOOL9 from subfamily A and PcaLOOL2 and PcaLOOL12 from subfamily B) were recombinantly produced and the purified proteins were characterized using diverse cellulose and chitin substrates. The purified PcaLOOLs weakened cellulose filter paper and cellulose nanofibril networks (CNF); however, none significantly boosted cellulase activity on the selected cellulose substrates (Avicel and Whatman paper). Although fusing the family 63 carbohydrate-binding module (CBM63) of BsEXLX1 encoded by Bacillus subtilis to PcaLOOLs increased their binding to cellulose, the CBM63 fusion appeared to reduce the cellulose filter paper weakening observed using wild-type proteins. Binding of PcaLOOLs to alpha-chitin was considerably higher than that to cellulose (Avicel) and was pH dependent, with the highest binding at pH 5.0. Amendment of certain PcaLOOLs in fungal liquid cultivations also impacted the density of the cultivated mycelia. The present study reveals the potential of fungal expansin-related proteins to impact both cellulose and chitin networks and points to a possible biological role in fungal cell wall processing.
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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 Socratic graph.