Evidence map›Paper›PMID 24031373›Full record

ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2009

Purification and characterization of extracellular lipase from a new strain: Pseudomonas aeruginosa SRT 9.

Prita S Borkar, Ragini G Bodade, Srinivasa R Rao, C N Khobragade

Open access · greenAbstract read
In one paragraph

Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 65 citations in OpenAlex.

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  9. Effect of mutation at oxyanion hole residu (H110F) on activity of Lk4 lipase.Biotechnology reports (Amsterdam, Netherlands) · 2021
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  16. Purification and characterization of lipase byJournal, genetic engineering & biotechnology · 2017
    Article
  17. Identification of lipolytic enzymes isolated from bacteria indigenous toBiotechnology reports (Amsterdam, Netherlands) · 2017
    Article
  18. Article
  19. Article
  20. An oxidant and organic solvent tolerant alkaline lipase by P. aeruginosa mutant: downstream processing and biochemical characterization.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2013
    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

4 authors at 1 institution in 1 country.

Prita S BorkarDepartment of Microbiology, N.E.S. Science college , Nanded - 431 605 , India ; School of Life Sciences, Biotechnology Research Laboratory, Swami Ramanand Teerth Marathwada University , Nanded - 431 606 , India.
Ragini G Bodade
Srinivasa R Rao
C N Khobragade
Swami Ramanand Teerth Marathwada University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An extra cellular lipase was isolated and purified from the culture broth of Pseudomonas aeruginosa SRT 9 to apparent homogeneity using ammonium sulfate precipitation followed by chromatographic techniques on phenyl Sepharose CL- 4B and Mono Q HR 5/5 column, resulting in a purification factor of 98 fold with specific activity of 12307.8 U/mg. The molecular weight of the purified lipase was estimated by SDS-PAGE to be 29 kDa with isoelectric point of 4.5. Maximum lipase activity was observed in a wide range of temperature and pH values with optimum temperature of 55ºC and pH 6.9. The lipase preferably acted on triacylglycerols of long chain (C14-C16) fatty acids. The lipase was inhibited strongly by EDTA suggesting the enzyme might be metalloprotein. SDS and metal ions such as Hg(2+), Zn(2+), Cu(2+), Ag(2+) and Fe(2+) decreased the lipase activity remarkedly. Its marked stability and activity in organic solvents suggest that this lipase is highly suitable as a biotechnological tool with a variety of applications including organo synthetic reactions and preparation of enantiomerically pure pharmaceuticals. The Km and Vmax value of the purified enzyme for triolein hydrolysis were calculated to be 1.11 mmol/L and 0.05 mmol/L/min respectively.

Indexed as

extra cellular lipasesMichaelis constantPseudomonas aeruginosa SRT9purification

Identifiers

PMID24031373
PMCPMC3769737
OpenAlexW2157022344

What OpenQuestion holds

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LicenceCC BY-NC
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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.