Evidence map›Paper›PMID 26528261›Full record

ArticleFrontiers in microbiology2015

A combined bioinformatics and functional metagenomics approach to discovering lipolytic biocatalysts.

Thorsten Masuch, Anna Kusnezowa, Sebastian Nilewski, José T Bautista, Robert Kourist, Lars I Leichert

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. The Impact of Metagenomics on Biocatalysis.Angewandte Chemie (International ed. in English) · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
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

6 authors at 1 institution in 1 country.

Thorsten MasuchDepartment of Microbial Biochemistry, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum Bochum, Germany.
Anna KusnezowaDepartment of Microbial Biochemistry, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum Bochum, Germany.
Sebastian NilewskiDepartment of Microbial Biochemistry, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum Bochum, Germany.
José T BautistaJunior Research Group for Microbial Biotechnology - Department for Biology and Biotechnology, Ruhr University Bochum Bochum, Germany.
Robert KouristJunior Research Group for Microbial Biotechnology - Department for Biology and Biotechnology, Ruhr University Bochum Bochum, Germany.
Lars I LeichertDepartment of Microbial Biochemistry, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum Bochum, Germany.
Ruhr University Bochum · DE

Funding

European Research Council 281384
6 · The paper itself

Abstract

The majority of protein sequence data published today is of metagenomic origin. However, our ability to assign functions to these sequences is often hampered by our general inability to cultivate the larger part of microbial species and the sheer amount of sequence data generated in these projects. Here we present a combination of bioinformatics, synthetic biology, and Escherichia coli genetics to discover biocatalysts in metagenomic datasets. We created a subset of the Global Ocean Sampling dataset, the largest metagenomic project published to date, by removing all proteins that matched Hidden Markov Models of known protein families from PFAM and TIGRFAM with high confidence (E-value > 10(-5)). This essentially left us with proteins with low or no homology to known protein families, still encompassing ~1.7 million different sequences. In this subset, we then identified protein families de novo with a Markov clustering algorithm. For each protein family, we defined a single representative based on its phylogenetic relationship to all other members in that family. This reduced the dataset to ~17,000 representatives of protein families with more than 10 members. Based on conserved regions typical for lipases and esterases, we selected a representative gene from a family of 27 members for synthesis. This protein, when expressed in E. coli, showed lipolytic activity toward para-nitrophenyl (pNP) esters. The K m-value of the enzyme was 66.68 μM for pNP-butyrate and 68.08 μM for pNP-palmitate with k cat/K m values at 3.4 × 10(6) and 6.6 × 10(5) M(-1)s(-1), respectively. Hydrolysis of model substrates showed enantiopreference for the R-form. Reactions yielded 43 and 61% enantiomeric excess of products with ibuprofen methyl ester and 2-phenylpropanoic acid ethyl ester, respectively. The enzyme retains 50% of its maximum activity at temperatures as low as 10°C, its activity is enhanced in artificial seawater and buffers with higher salt concentrations with an optimum osmolarity of 3,890 mosmol/l.

Indexed as

biocatalystesterasefunctional metagenomicslipasemetagenomics

Identifiers

PMID26528261
PMCPMC4602143
OpenAlexW2186025959

What OpenQuestion holds

Textmetadata
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.