ArticleThe Journal of biological chemistry2015
Novel β-1,4-Mannanase Belonging to a New Glycoside Hydrolase Family in Aspergillus nidulans.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 62 citations in OpenAlex.
- Structural Characterization and Engineering of a GH134 β-Mannanase from Aspergillus nidulans for Enhancement of Activity and Stability.Journal of agricultural and food chemistry · 2026Article
- Improved thermostability of Thermobifida fusca mannanase obtained by error-prone PCR mutagenesis.Biotechnology letters · 2026Article
- Biochemical characterization of the α-1,3-mannosidase AnGH92A from Aspergillus nidulans.Scientific reports · 2026Article
- Harnessing magnetic cross-linked cell aggregates (CLCAs) for cost-effective preparation of Konjac mannan-oligosaccharide.Microbial cell factories · 2025Article
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- Towards an understanding of the enzymatic degradation of complex plant mannan structures.World journal of microbiology & biotechnology · 2023Review
- Biochemical Characterization of a Pectate Lyase AnPL9 from Aspergillus nidulans.Applied biochemistry and biotechnology · 2022Article
- Reshaping the binding channel of a novel GH113 family β-mannanase from Paenibacillus cineris (PcMan113) for enhanced activity.Bioresources and bioprocessing · 2022Article
- Article
- Enzymatic Conversion of Mannan-Rich Plant Waste Biomass into Prebiotic Mannooligosaccharides.Foods (Basel, Switzerland) · 2021Review
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Expression, homology modeling and enzymatic characterization of a new β-mannanase belonging to glycoside hydrolase family 1 from Enterobacter aerogenes B19.Microbial cell factories · 2020Article
- Characterization of FsXEG12A from the cellulose-degrading ectosymbiotic fungus Fusarium spp. strain EI cultured by the ambrosia beetle.AMB Express · 2020Article
- Oxygen radical based on non-thermal atmospheric pressure plasma alleviates lignin-derived phenolic toxicity in yeast.Biotechnology for biofuels · 2020Article
- Ability of Saccharomyces cerevisiae MC87-46 to assimilate isomaltose and its effects on sake taste.Scientific reports · 2019Article
- Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications.World journal of microbiology & biotechnology · 2019Review
- Oxygen-radical pretreatment promotes cellulose degradation by cellulolytic enzymes.Biotechnology for biofuels · 2017Article
- Network reconstruction and systems analysis of plant cell wall deconstruction byBiotechnology for biofuels · 2017Article
- Diversity of microbial carbohydrate-active enzymes in Danish anaerobic digesters fed with wastewater treatment sludge.Biotechnology for biofuels · 2017Article
- Directed evolution of a β-mannanase fromBiotechnology for biofuels · 2017Article
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many filamentous fungi produce β-mannan-degrading β-1,4-mannanases that belong to the glycoside hydrolase 5 (GH5) and GH26 families. Here we identified a novel β-1,4-mannanase (Man134A) that belongs to a new glycoside hydrolase (GH) family (GH134) in Aspergillus nidulans. Blast analysis of the amino acid sequence using the NCBI protein database revealed that this enzyme had no similarity to any sequences and no putative conserved domains. Protein homologs of the enzyme were distributed to limited fungal and bacterial species. Man134A released mannobiose (M2), mannotriose (M3), and mannotetraose (M4) but not mannopentaose (M5) or higher manno-oligosaccharides when galactose-free β-mannan was the substrate from the initial stage of the reaction, suggesting that Man134A preferentially reacts with β-mannan via a unique catalytic mode. Man134A had high catalytic efficiency (kcat/Km) toward mannohexaose (M6) compared with the endo-β-1,4-mannanase Man5C and notably converted M6 to M2, M3, and M4, with M3 being the predominant reaction product. The action of Man5C toward β-mannans was synergistic. The growth phenotype of a Man134A disruptant was poor when β-mannans were the sole carbon source, indicating that Man134A is involved in β-mannan degradation in vivo. These findings indicate a hitherto undiscovered mechanism of β-mannan degradation that is enhanced by the novel β-1,4-mannanase, Man134A, when combined with other mannanolytic enzymes including various endo-β-1,4-mannanases.
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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 OpenQuestion graph.