Evidence map›Paper›PMID 37036659›Full record

ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2023

Characterization of L-asparaginase from Streptomyces koyangensis SK4 with acrylamide-minimizing potential in potato chips.

S Shahana Kabeer, Bini Francis, S Vishnupriya, Hafsa Kattatheyil, K J Joseph, K P Krishnan, A A Mohamed Hatha

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

2 citing papers in PubMed, 11 citations in OpenAlex.

  1. l-Asparaginase fromACS omega · 2024
    Article
  2. 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

7 authors at 1 institution in 1 country.

S Shahana KabeerDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kochi, Kerala, India. sakabeer37@gmail.com.
Bini FrancisDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kochi, Kerala, India.
S VishnupriyaDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kochi, Kerala, India.
Hafsa KattatheyilDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kochi, Kerala, India.
K J JosephDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kochi, Kerala, India.
K P KrishnanNational Centre for Polar and Ocean Research, Vasco da Gama, Goa, India.
A A Mohamed HathaDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Kochi, Kerala, India.
Cochin University of Science and Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial L-asparaginase is well known for its application in food industries to reduce acrylamide content in fried starchy food. L-asparaginase produced by Arctic actinomycetes Streptomyces koyangensis SK4 was purified and studied for biochemical characterization. The L-asparaginase was purified with a yield of 15.49% and final specific activity of 179.77 IU/mg of protein. The enzyme exhibited a molecular weight of 43 kDa. The optimum pH and temperature for maximum activity of the purified enzyme were 8.5 °C and 40 °C, respectively. The enzyme expressed maximum activity at an incubation period of 30 min and a substrate concentration of 0.06 M. The enzyme has a low Km value of 0.041 M and excellent substrate specificity toward L-asparagine. The enzyme activity was inhibited by metal ions Ba

Indexed as

AsparaginaseStreptomycesAcrylamideTemperatureAcrylamideAsparaginaseAcrylamide reductionArctic actinomycetesCharacterizationL-asparaginasePurification

Identifiers

PMID37036659
PMCPMC10485229
OpenAlexW4363646644

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.