ArticleApplied microbiology and biotechnology2014
An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5.
Article in Applied microbiology and biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 49 citations in OpenAlex.
- Discovery and Characterization of Mannan-Specialized GH5 Endo-1,4-β-mannanases: a Strategy for Açaí (Journal of agricultural and food chemistry · 2025Article
- Article
- Biochemical analyses of a novel acidophilic GH5 β-mannanase fromFrontiers in microbiology · 2023Article
- Molecular insight into Aspergillus oryzae β-mannanase interacting with mannotriose revealed by molecular dynamic simulation study.PloS one · 2022Article
- Crystal structure of a homotrimeric verrucomicrobialJournal of structural biology: X · 2021Article
- Crystal structure and substrate interactions of an unusual fungal non-CBM carrying GH26 endo-β-mannanase from Yunnania penicillata.Scientific reports · 2019Article
- Production and purification of mannan oligosaccharide with epithelial tight junction enhancing activity.PeerJ · 2019Article
- Structural insights into the catalytic mechanism of a novel glycoside hydrolase family 113 β-1,4-mannanase fromThe Journal of biological chemistry · 2018Article
- β-Mannanase-catalyzed synthesis of alkyl mannooligosides.Applied microbiology and biotechnology · 2018Article
- A Novel Glycoside Hydrolase Family 113 Endo-β-1,4-Mannanase from Alicyclobacillus sp. Strain A4 and Insight into the Substrate Recognition and Catalytic Mechanism of This Family.Applied and environmental microbiology · 2016Article
- Novel β-1,4-Mannanase Belonging to a New Glycoside Hydrolase Family in Aspergillus nidulans.The Journal of biological chemistry · 2015Article
- The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes.BMC biochemistry · 2015Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Mannanases are involved in the conversion and modification of mannan-based saccharides. Using a retaining mechanism, they can, in addition to hydrolysis, also potentially perform transglycosylation reactions, synthesizing new glyco-conjugates. Transglycosylation has been reported for β-mannanases in GH5 and GH113. However, although they share the same fold and catalytic mechanism, there may be differences in the enzymes' ability to perform transglycosylation. Three GH5 β-mannanases from Aspergillus nidulans, AnMan5A, AnMan5B and AnMan5C, which belong to subfamily GH5_7 were studied. Comparative studies, including the GH5_7 TrMan5A from Trichoderma reesei, showed some differences between the enzymes. All the enzymes could perform transglycosylation but AnMan5B stood out in generating comparably higher amounts of transglycosylation products when incubated with manno-oligosaccharides. In addition, AnMan5B did not use alcohols as acceptor, which was also different compared to the other three β-mannanases. In order to map the preferred binding of manno-oligosaccharides, incubations were performed in H2 (18)O. AnMan5B in contrary to the other enzymes did not generate any (18)O-labelled products. This further supported the idea that AnMan5B potentially prefers to use saccharides as acceptor instead of water. A homology model of AnMan5B showed a non-conserved Trp located in subsite +2, not present in the other studied enzymes. Strong aglycone binding seems to be important for transglycosylation with saccharides. Depending on the application, it is important to select the right enzyme.
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