Evidence map›Paper›PMID 23180548›Full record

ArticleWorld journal of microbiology & biotechnology2013

Purification, characterization and kinetic properties of extracellular L-asparaginase produced by Cladosporium sp.

N S Mohan Kumar, H K Manonmani

Abstract read
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In one paragraph

Article in World journal of microbiology & biotechnology, 2013. 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
10.5field-weighted citation impact, top 2% 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, 101 citations in OpenAlex.

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  10. Characterization of L-asparaginase from Streptomyces koyangensis SK4 with acrylamide-minimizing potential in potato chips.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
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  14. Characterization of a Novel L-Asparaginase fromFoods (Basel, Switzerland) · 2021
    Article
  15. Article
  16. Review
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  18. What makes a good new therapeutic L-asparaginase?World journal of microbiology & biotechnology · 2019
    Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

N S Mohan KumarFermentation Technology and Bioengineering Department, Central Food Technological Research Institute (CFTRI), Mysore 570 020, India.
H K Manonmani
Central Food Technological Research Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-asparaginase from Cladosporium sp. grown on wheat bran by SSF was purified. Enzyme appeared to be a trimer with homodimer of 37 kDa and another 47 kDa amounting to total mass of 121 kDa as estimated by SDS-PAGE and 120 kDa on gel filtration column. The optimum temperature and pH of the enzyme were 30 °C and 6.3, respectively with Vmax of 4.44 μmol/mL/min and Km of 0.1 M. Substrate specificity studies indicated that, L-asparaginase has greater affinity towards L-asparagine with substrate hydrolysis efficiency (Vmax/Km ratio) eightfold higher than that of L-glutamine. L-asparaginase activity in presence of thiols studied showed decrease in Vmax and increase in Km, indicating nonessential mode of inactivation. Among the thiols tested, β-mercaptomethanol, exerted inhibitory effect, suggesting a critical role of disulphide linkages in maintaining a suitable conformation of the enzyme. Metal ions such as Ca(2+), Co(2+), Cu(2+), Mg(2+), Na(+), K(+) and Zn(2+) significantly affected enzyme activity whereas presence of Fe(3+), Pb(2+) and KI stimulated the activity. Detergents studied also enhanced L-asparaginase activity. In-vitro half-life of purified L-asparaginase in mammalian blood serum was 93.69 h. The enzyme inhibited acrylamide formation in potato chips by 96 % making it a potential candidate for food industry to reduce acrylamide content in starchy fried food commodities.

Indexed as

AsparaginaseAsparagineChromatography, GelCladosporiumCulture MediaElectrophoresis, Polyacrylamide GelEnzyme ActivatorsEnzyme InhibitorsEnzyme StabilityGlutamineHydrogen-Ion ConcentrationKineticsMolecular WeightProtein MultimerizationSubstrate SpecificityTemperatureAsparaginaseAsparagineCulture MediaEnzyme ActivatorsEnzyme InhibitorsGlutamine

Identifiers

PMID23180548
OpenAlexW2088141280

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.