↓ Skip to main content

Multifunctional cellulase catalysis targeted by fusion to different carbohydrate-binding modules

Overview of attention for article published in Biotechnology for Biofuels, December 2015
Altmetric Badge

About this Attention Score

  • Above-average Attention Score compared to outputs of the same age (60th percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

twitter
3 tweeters
facebook
1 Facebook page

Citations

dimensions_citation
25 Dimensions

Readers on

mendeley
73 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Multifunctional cellulase catalysis targeted by fusion to different carbohydrate-binding modules
Published in
Biotechnology for Biofuels, December 2015
DOI 10.1186/s13068-015-0402-0
Pubmed ID
Authors

Johnnie A. Walker, Taichi E. Takasuka, Kai Deng, Christopher M. Bianchetti, Hannah S. Udell, Ben M. Prom, Hyunkee Kim, Paul D. Adams, Trent R. Northen, Brian G. Fox

Abstract

Carbohydrate binding modules (CBMs) bind polysaccharides and help target glycoside hydrolases catalytic domains to their appropriate carbohydrate substrates. To better understand how CBMs can improve cellulolytic enzyme reactivity, representatives from each of the 18 families of CBM found in Ruminoclostridium thermocellum were fused to the multifunctional GH5 catalytic domain of CelE (Cthe_0797, CelEcc), which can hydrolyze numerous types of polysaccharides including cellulose, mannan, and xylan. Since CelE is a cellulosomal enzyme, none of these fusions to a CBM previously existed. CelEcc_CBM fusions were assayed for their ability to hydrolyze cellulose, lichenan, xylan, and mannan. Several CelEcc_CBM fusions showed enhanced hydrolytic activity with different substrates relative to the fusion to CBM3a from the cellulosome scaffoldin, which has high affinity for binding to crystalline cellulose. Additional binding studies and quantitative catalysis studies using nanostructure-initiator mass spectrometry (NIMS) were carried out with the CBM3a, CBM6, CBM30, and CBM44 fusion enzymes. In general, and consistent with observations of others, enhanced enzyme reactivity was correlated with moderate binding affinity of the CBM. Numerical analysis of reaction time courses showed that CelEcc_CBM44, a combination of a multifunctional enzyme domain with a CBM having broad binding specificity, gave the fastest rates for hydrolysis of both the hexose and pentose fractions of ionic-liquid pretreated switchgrass. We have shown that fusions of different CBMs to a single multifunctional GH5 catalytic domain can increase its rate of reaction with different pure polysaccharides and with pretreated biomass. This fusion approach, incorporating domains with broad specificity for binding and catalysis, provides a new avenue to improve reactivity of simple combinations of enzymes within the complexity of plant biomass.

Twitter Demographics

The data shown below were collected from the profiles of 3 tweeters 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 73 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Japan 1 1%
Brazil 1 1%
Unknown 71 97%

Demographic breakdown

Readers by professional status Count As %
Researcher 20 27%
Student > Ph. D. Student 18 25%
Student > Master 9 12%
Student > Doctoral Student 7 10%
Student > Bachelor 5 7%
Other 8 11%
Unknown 6 8%
Readers by discipline Count As %
Agricultural and Biological Sciences 36 49%
Biochemistry, Genetics and Molecular Biology 11 15%
Chemical Engineering 5 7%
Engineering 3 4%
Chemistry 3 4%
Other 7 10%
Unknown 8 11%

Attention Score in Context

This research output has an Altmetric Attention Score of 3. 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 29 February 2016.
All research outputs
#2,975,633
of 7,313,486 outputs
Outputs from Biotechnology for Biofuels
#198
of 567 outputs
Outputs of similar age
#108,994
of 283,613 outputs
Outputs of similar age from Biotechnology for Biofuels
#13
of 22 outputs
Altmetric has tracked 7,313,486 research outputs across all sources so far. This one has received more attention than most of these and is in the 58th percentile.
So far Altmetric has tracked 567 research outputs from this source. They receive a mean Attention Score of 3.8. This one has gotten more attention than average, scoring higher than 64% of its peers.
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 283,613 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 60% of its contemporaries.
We're also able to compare this research output to 22 others from the same source and published within six weeks on either side of this one. This one is in the 40th percentile – i.e., 40% of its contemporaries scored the same or lower than it.