ArticleThe Journal of biological chemistry2016
Identification of the Gene Encoding Isoprimeverose-producing Oligoxyloglucan Hydrolase in Aspergillus oryzae.
Article in The Journal of biological chemistry, 2016. 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, 35 citations in OpenAlex.
- Fungal Rutinosidase─Engineering of a Side Tunnel Steers Its Transglycosylation Potential.Journal of agricultural and food chemistry · 2026Article
- Characterization of glycoside hydrolases involved in xyloglucan degradation in the thermophilic bacterium Thermotoga maritima.Scientific reports · 2025Article
- Production of Isoprimeverose from Xyloglucan UsingJournal of applied glycoscience · 2025Article
- Identity of Carbohydrate-Responsive Genes in a Cultured Microbial Community Using Metagenomic and Metatranscriptomic Approaches.Journal of applied glycoscience · 2025Article
- Identification and Characterization of Novel Intracellular α-Xylosidase inJournal of applied glycoscience · 2023Article
- Characterization of an extracellular α-xylosidase involved in xyloglucan degradation in Aspergillus oryzae.Applied microbiology and biotechnology · 2022Article
- Enzymatic degradation of xyloglucans by Aspergillus species: a comparative view of this genus.Applied microbiology and biotechnology · 2021Review
- Aspergillus oryzae Rutinosidase: Biochemical and Structural Investigation.Applied and environmental microbiology · 2021Article
- A novel isoprimeverose-producing enzyme fromFEBS open bio · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aspergillus oryzae produces a unique β-glucosidase, isoprimeverose-producing oligoxyloglucan hydrolase (IPase), that recognizes and releases isoprimeverose (α-D-xylopyranose-(1 → 6)-D-glucopyranose) units from the non-reducing ends of oligoxyloglucans. A gene encoding A. oryzae IPase, termed ipeA, was identified and expressed in Pichia pastoris. With the exception of cellobiose, IpeA hydrolyzes a variety of oligoxyloglucans and is a member of the glycoside hydrolase family 3. Xylopyranosyl branching at the non-reducing ends was vital for IPase activity, and galactosylation at a α-1,6-linked xylopyranosyl side chain completely abolished IpeA activity. Hepta-oligoxyloglucan saccharide (Xyl3Glc4) substrate was preferred over tri- (Xyl1Glc2) and tetra- (Xyl2Glc2) oligoxyloglucan saccharides substrates. IpeA transferred isoprimeverose units to other saccharides, indicating transglycosylation activity. The ipeA gene was expressed in xylose and xyloglucan media and was strongly induced in the presence of xyloglucan endo-xyloglucanase-hydrolyzed products. This is the first study to report the identification of a gene encoding IPase in eukaryotes.
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