Evidence map›Paper›PMID 27478501›Full record

ArticleBiotechnology for biofuels2016

Cell-free synthesis of functional phospholipase A1 from Serratia sp.

Hye Jin Lim, Yu Jin Park, Yeon Jae Jang, Ji Eun Choi, Joon Young Oh, Ji Hyun Park, Jae Kwang Song, Dong-Myung Kim

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. A Cost-EffectiveBioengineering (Basel, Switzerland) · 2024
    Article
  3. High-Throughput Experimentation Using Cell-Free Protein Synthesis Systems.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  4. Review
  5. Article
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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

8 authors at 2 institutions in 1 country.

Hye Jin LimDepartment of Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon, 305-764 Republic of Korea ; Research Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology, Daejeon, 305-600 Republic of Korea.
Yu Jin ParkDepartment of Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon, 305-764 Republic of Korea.
Yeon Jae JangDepartment of Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon, 305-764 Republic of Korea.
Ji Eun ChoiResearch Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology, Daejeon, 305-600 Republic of Korea.
Joon Young OhResearch Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology, Daejeon, 305-600 Republic of Korea.
Ji Hyun ParkResearch Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology, Daejeon, 305-600 Republic of Korea.
Jae Kwang SongResearch Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology, Daejeon, 305-600 Republic of Korea.
Dong-Myung KimDepartment of Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon, 305-764 Republic of Korea.ORCID 0000-0001-7875-0694
Chungnam National University · KRKorea Research Institute of Chemical Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPhospholipase A1 is an enzyme that hydrolyzes phospholipids at the sn-1 position. It has potential applications across diverse fields including food, pharmaceutical, and biofuel industries. Although there has been increasing interest in the use of phospholipase A1 for degumming of plant oils during biodiesel production, production of recombinant phospholipase A1 has been hampered by low efficiency of gene expression and its toxicity to the host cell.

resultsWhile expression of phospholipase A1 in Escherichia coli resulted in extremely low productivity associated with inhibition of transformed cell growth, drastically higher production of functional phospholipase A1 was achieved in a cell-free protein synthesis system where enzyme expression is decoupled from cell physiology. Compared with expression in E. coli, cell-free synthesis resulted in an over 1000-fold higher titer of functional phospholipase A1. Cell-free produced phospholipase A1 was also used for successfully degumming crude plant oil.

conclusionsWe demonstrate successful production of Serratia sp. phospholipase A1 in a cell-free protein synthesis system. Including the phospholipase A1 investigated in this study, many industrial enzymes can interfere with the regular physiology of cells, making cellular production of them problematic. With the experimental results presented herewith, we believe that cell-free protein synthesis will provide a viable option for rapid production of important industrial biocatalysts.

Indexed as

BiodieselCell-free protein synthesisEnzymatic degummingIndustrial enzymesPhospholipase A1

Identifiers

PMID27478501
PMCPMC4966862
OpenAlexW2500108654

What OpenQuestion holds

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LicenceCC BY
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.