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Expression of the Thermobifida fusca xylanase Xyn11A in Pichia pastoris and its characterization

Overview of attention for article published in BMC Biotechnology, March 2015
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  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (84th percentile)
  • Average Attention Score compared to outputs of the same age and source

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Title
Expression of the Thermobifida fusca xylanase Xyn11A in Pichia pastoris and its characterization
Published in
BMC Biotechnology, March 2015
DOI 10.1186/s12896-015-0135-y
Pubmed ID
Authors

Longmei Zhao, Jiang Geng, Yaoqi Guo, Xiudong Liao, Xuhui Liu, Rujuan Wu, Zhaojun Zheng, Rijun Zhang

Abstract

Xylan is a major component of plant cells and the most abundant hemicellulose. Xylanases degrade xylan into monomers by randomly cleaving β-1,4-glycosidic bonds in the xylan backbone, and have widespread potential applications in various industries. The purpose of our study was to clone and express the endoxylanase gene xynA of Thermobifida fusca YX in its native form and with a C-terminal histidine (His) tag in Pichia pastoris X-33. We analyzed and compared these two forms of the protein and examined their potential applications in various industries. The xynA gene from T. fusca YX was successfully cloned and expressed using P. pastoris X-33. We produced a recombinant native form of the protein (rXyn11A) and a C-terminal His-tagged form of the desired protein (rXyn11A-(His)6). The specific activities of rXyn11A and rXyn11A-(His)6 in culture supernatants approached 149.4 and 133.4 U/mg, respectively. These activities were approximately 4- and 3.5-fold higher than those for the non-recombinant wild-type Xyn11A (29.3 U/mg). Following purification, the specific activities of rXyn11A and rXyn11A-(His)6 were 557.35 and 515.84 U/mg, respectively. The specific activity of rXyn11A was 8% higher than that of rXyn11A-(His)6. Both recombinant xylanases were optimally active at 80°C and pH 8.0, and exhibited greater than 60% activity between pH 6-9 and 60-80°C. They exhibited similar pH stability, while rXyn11A exhibited better thermostability; N-glycosylation enhanced the thermostability of both recombinant xylanases. The products of beechwood xylan hydrolyzed by both xylanases included xylobiose, xylotriose, xylotetraose and xylopentaose. The C-terminal His tag had adverse effects when added to the Xyn11A protein. The thermostability of both recombinant xylanases was enhanced by N-glycosylation. Their stabilities at a high pH and temperature indicate their potential for application in various industries.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 39 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
China 1 3%
Unknown 38 97%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 11 28%
Researcher 6 15%
Student > Master 4 10%
Other 3 8%
Student > Bachelor 3 8%
Other 6 15%
Unknown 6 15%
Readers by discipline Count As %
Agricultural and Biological Sciences 15 38%
Biochemistry, Genetics and Molecular Biology 12 31%
Unspecified 1 3%
Business, Management and Accounting 1 3%
Arts and Humanities 1 3%
Other 4 10%
Unknown 5 13%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 10. 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 25 February 2016.
All research outputs
#2,937,933
of 22,796,179 outputs
Outputs from BMC Biotechnology
#119
of 935 outputs
Outputs of similar age
#42,983
of 286,004 outputs
Outputs of similar age from BMC Biotechnology
#14
of 27 outputs
Altmetric has tracked 22,796,179 research outputs across all sources so far. Compared to these this one has done well and is in the 86th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 935 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 7.7. This one has done well, scoring higher than 85% 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 286,004 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 84% of its contemporaries.
We're also able to compare this research output to 27 others from the same source and published within six weeks on either side of this one. This one is in the 33rd percentile – i.e., 33% of its contemporaries scored the same or lower than it.