ArticleThe Journal of biological chemistry2011
Biochemical and molecular characterization of secreted α-xylosidase from Aspergillus niger.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- 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
- Crystal Structure of α-Xylosidase fromACS sustainable chemistry & engineering · 2020Article
- Analysis of Transglucosylation Products ofJournal of applied glycoscience · 2020Article
- Target highlights in CASP13: Experimental target structures through the eyes of their authors.Proteins · 2019Article
- Soluble and Membrane-Bound β-Glucosidases Are Involved in Trimming the Xyloglucan Backbone.Plant physiology · 2017Article
- Article
- Factors contributing to the recalcitrance of herbaceous dicotyledons (forbs) to enzymatic deconstruction.Biotechnology for biofuels · 2014Article
- Article
- Enhancement of fermentable sugar yields by α-xylosidase supplementation of commercial cellulases.Biotechnology for biofuels · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Linked xylose is a major component of xyloglucans in the cell walls of higher plants. An α-xylosidase (AxlA) was purified from a commercial enzyme preparation from Aspergillus niger, and the encoding gene was identified. The protein is a member of glycosyl hydrolase family 31. It was active on p-nitrophenyl-α-d-xyloside, isoprimeverose, xyloglucan heptasaccharide (XXXG), and tamarind xyloglucan. When expressed in Pichia pastoris, AxlA had activity comparable to the native enzyme on pNPαX and IP despite apparent hyperglycosylation. The pH optimum of AxlA was between 3.0 and 4.0. AxlA together with β-glucosidase depolymerized xyloglucan heptasaccharide. A combination of AxlA, β-glucosidase, xyloglucanase, and β-galactosidase in the optimal proportions of 51:5:19:25 or 59:5:11:25 could completely depolymerize tamarind XG to free Glc or Xyl, respectively. To the best of our knowledge, this is the first characterization of a secreted microbial α-xylosidase. Secreted α-xylosidases appear to be rare in nature, being absent from other tested commercial enzyme mixtures and from the genomes of most filamentous fungi.
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.