ArticleSpringerPlus2016
Is it possible to optimize the protein production yield by the generation of homomultimeric fusion enzymes?
Article in SpringerPlus, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed, 6 citations in OpenAlex.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe supply of industrially relevant biocatalysts demands an easy and efficient protein production in high yield. In a conventional approach, a recombinant protein is produced in a heterologous host enabling the manipulation of multiple parameters including expression plasmids, growth conditions and regulation of protein biosynthesis. In this study, the generation of homomultimeric fusion genes is tested as an additional parameter to increase the production yield of a heat-stable cellulase.
findingsThe LE (LguI/Eco81I)-cloning strategy was used to generate a set of plasmids containing a single copy or two to four repetitions of the endoglucanase-encoding gene cel5A from the thermophilic anaerobe Fervidobacterium gondwanense. Serial up-scaling of shaking flask volumes from 50 to 500 mL were used to determine the production yield of active cellulolytic enzyme Cel5A in recombinant form in Escherichia coli. Monitoring the cellular wet weight and total protein proved that the bacterial growth rate is not depending on the production of fusion enzymes, however activity assays in combination with Western blotting analyses indicated instability effects of large homomultimeric fusion enzymes.
conclusionThe production yield of fusion cellulases is constant with increasing molecular weights, but improved activities were not observed for recombinant Cel5A homomultimers. This strategy may serve as a starting point for further studies to generate more stable fusion proteins with improved catalytic activities and higher protein yield in the future.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.