Evidence map›Paper›PMID 9925602›Full record

ArticleApplied and environmental microbiology1999

Purification and properties of a xylan-binding endoxylanase from Alkaliphilic bacillus sp. strain K-1.

K Ratanakhanokchai, K L Kyu, M Tanticharoen

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.9field-weighted citation impact, top 7% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 165 citations in OpenAlex.

  1. Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Alkaliphilic bacteria: applications in industrial biotechnology.Journal of industrial microbiology & biotechnology · 2011
    Review
  17. Article
  18. One-step purification and characterization of cellulase-free xylanase produced by alkalophilic Bacillus subtilis ash.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2010
    Article
  19. Biosynthesis of selenium nanoparticles using Klebsiella pneumoniae and their recovery by a simple sterilization process.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2010
    Article
  20. Multimeric hemicellulases facilitate biomass conversion.Applied and environmental microbiology · 2009
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

K RatanakhanokchaiSchool of Bioresources and Technology, King Mongkut's University of Technology, Thonburi, Bangkok 10140, Thailand. ikhachai@cc.kmitt.ac.th
K L Kyu
M Tanticharoen
King Mongkut's University of Technology Thonburi · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An alkaliphilic bacterium, Bacillus sp. strain K-1, produces extracellular xylanolytic enzymes such as xylanases, beta-xylosidase, arabinofuranosidase, and acetyl esterase when grown in xylan medium. One of the extracellular xylanases that is stable in an alkaline state was purified to homogeneity by affinity adsorption-desorption on insoluble xylan. The enzyme bound to insoluble xylan but not to crystalline cellulose. The molecular mass of the purified xylan-binding xylanase was estimated to be approximately 23 kDa. The enzyme was stable at alkaline pHs up to 12. The optimum temperature and optimum pH of the enzyme activity were 60 degrees C and 5.5, respectively. Metal ions such as Fe2+, Ca2+, and Mg2+ greatly increased the xylanase activity, whereas Mn2+ strongly inhibited it. We also demonstrated that the enzyme could hydrolyze the raw lignocellulosic substances effectively. The enzymatic products of xylan hydrolysis were a series of short-chain xylooligosaccharides, indicating that the enzyme was an endoxylanase.

Identifiers

PMID9925602
PMCPMC91081
OpenAlexW2118700334

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.