Evidence map›Paper›PMID 24947581›Full record

ArticleJournal of industrial microbiology & biotechnology2014

A novel approach for improving the yield of Bacillus subtilis transglutaminase in heterologous strains.

Yihan Liu, Song Lin, Xiqing Zhang, Xiaoguang Liu, Jianling Wang, Fuping Lu

Abstract read
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In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 39 citations in OpenAlex.

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  5. Crosslinking Mechanism on a NovelFoods (Basel, Switzerland) · 2022
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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

6 authors at 2 institutions in 1 country.

Yihan LiuKey Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, National Engineering Laboratory for Industrial Enzymes, The College of Biotechnology, Tianjin University of Science and Technology, Tianjin, People's Republic of China.
Song Lin
Xiqing Zhang
Xiaoguang Liu
Jianling Wang
Fuping Lu
Tianjin University of Science and Technology · CNTianjin Economic-Technological Development Area · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transglutaminase (BTG) from Bacillus subtilis is considered to be a new type of transglutaminase for the food industry. Given that the BTG gene only encodes a mature peptide, the expression of BTG in heterologous microbial hosts could affect their normal growth due to BTG's typical transglutaminase activity which can catalyze cross-linking of proteins in the cells. Therefore, we developed a novel approach to suppress BTG activity and reduce the toxicity on microbial hosts, thus improving BTG yield. Genes encoding the respective regions of transglutaminase propeptide from seven species of Streptomyces were fused to the N-terminal of the BTG gene to produce fusion proteins. We found that all the fused propeptides could suppress BTG activity. Importantly, BTG activity could be completely restored after the removal of the propeptides by proteolytic cleavage. Of the seven propeptides tested, the propeptide proD from Streptomyces caniferus had the strongest suppressive effect on BTG activity (70 % of the activity suppressed). Moreover, fusion protein proD-BTG (containing proD) also exhibited the highest yield which was more than twofold of the expression level of BTG in an active form in Escherichia coli. Secretion expression of BTG and proD-BTG in Corynebacterium glutamicum further showed that our novel approach was suitable for the efficient BTG expression, thus providing a valuable platform for further optimization of large-scale BTG production.

Indexed as

BioreactorsAmino Acid SequenceBacillus subtilisCorynebacterium glutamicumElectrophoresis, Polyacrylamide GelEnzyme PrecursorsEscherichia coliIndustrial MicrobiologyMolecular Sequence DataPlasmidsRecombinant Fusion ProteinsRosaniline DyesStreptomycesTransglutaminasescoomassie Brilliant BlueEnzyme PrecursorsRecombinant Fusion ProteinsRosaniline DyesTransglutaminases

Identifiers

PMID24947581
OpenAlexW2051448658

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.