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Enhancement of cellulosome-mediated deconstruction of cellulose by improving enzyme thermostability

Overview of attention for article published in Biotechnology for Biofuels, August 2016
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Title
Enhancement of cellulosome-mediated deconstruction of cellulose by improving enzyme thermostability
Published in
Biotechnology for Biofuels, August 2016
DOI 10.1186/s13068-016-0577-z
Pubmed ID
Authors

Sarah Moraïs, Johanna Stern, Amaranta Kahn, Anastasia P. Galanopoulou, Shahar Yoav, Melina Shamshoum, Matthew A. Smith, Dimitris G. Hatzinikolaou, Frances H. Arnold, Edward A. Bayer

Abstract

The concerted action of three complementary cellulases from Clostridium thermocellum, engineered to be stable at elevated temperatures, was examined on a cellulosic substrate and compared to that of the wild-type enzymes. Exoglucanase Cel48S and endoglucanase Cel8A, both key elements of the natural cellulosome from this bacterium, were engineered previously for increased thermostability, either by SCHEMA, a structure-guided, site-directed protein recombination method, or by consensus-guided mutagenesis combined with random mutagenesis using error-prone PCR, respectively. A thermostable β-glucosidase BglA mutant was also selected from a library generated by error-prone PCR that will assist the two cellulases in their methodic deconstruction of crystalline cellulose. The effects of a thermostable scaffoldin versus those of a largely mesophilic scaffoldin were also examined. By improving the stability of the enzyme subunits and the structural component, we aimed to improve cellulosome-mediated deconstruction of cellulosic substrates. The results demonstrate that the combination of thermostable enzymes as free enzymes and a thermostable scaffoldin was more active on the cellulosic substrate than the wild-type enzymes. Significantly, "thermostable" designer cellulosomes exhibited a 1.7-fold enhancement in cellulose degradation compared to the action of conventional designer cellulosomes that contain the respective wild-type enzymes. For designer cellulosome formats, the use of the thermostabilized scaffoldin proved critical for enhanced enzymatic performance under conditions of high temperatures. Simple improvement in the activity of a given enzyme does not guarantee its suitability for use in an enzyme cocktail or as a designer cellulosome component. The true merit of improvement resides in its ultimate contribution to synergistic action, which can only be determined experimentally. The relevance of the mutated thermostable enzymes employed in this study as components in multienzyme systems has thus been confirmed using designer cellulosome technology. Enzyme integration via a thermostable scaffoldin is critical to the ultimate stability of the complex at higher temperatures. Engineering of thermostable cellulases and additional lignocellulosic enzymes may prove a determinant parameter for development of state-of-the-art designer cellulosomes for their employment in the conversion of cellulosic biomass to soluble sugars.Graphical abstractConversion of conventional designer cellulosomes into thermophilic designer cellulosomes.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 98 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Japan 1 1%
Unknown 97 99%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 23 23%
Student > Master 18 18%
Researcher 17 17%
Student > Doctoral Student 9 9%
Student > Bachelor 9 9%
Other 13 13%
Unknown 9 9%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 36 37%
Agricultural and Biological Sciences 28 29%
Chemistry 8 8%
Chemical Engineering 4 4%
Immunology and Microbiology 2 2%
Other 7 7%
Unknown 13 13%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 07 August 2016.
All research outputs
#7,077,149
of 8,177,609 outputs
Outputs from Biotechnology for Biofuels
#573
of 668 outputs
Outputs of similar age
#217,485
of 257,543 outputs
Outputs of similar age from Biotechnology for Biofuels
#19
of 19 outputs
Altmetric has tracked 8,177,609 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 668 research outputs from this source. They receive a mean Attention Score of 4.0. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 257,543 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 19 others from the same source and published within six weeks on either side of this one. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.