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A trehalase from Zunongwangia sp.: characterization and improving catalytic efficiency by directed evolution

Overview of attention for article published in BMC Biotechnology, January 2016
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  • Good Attention Score compared to outputs of the same age (73rd percentile)

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2 tweeters
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1 patent

Citations

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14 Mendeley
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Title
A trehalase from Zunongwangia sp.: characterization and improving catalytic efficiency by directed evolution
Published in
BMC Biotechnology, January 2016
DOI 10.1186/s12896-016-0239-z
Pubmed ID
Authors

Qipeng Cheng, Haofeng Gao, Nan Hu

Abstract

Trehalases have potential applications in several fields, including food additives, insecticide development, and transgenic plant. In the present study, we focused on a trehalase from the marine bacterium Zunongwangia sp., which hydrolyzes trehalose to glucose. A novel gene, treZ (1590 bp) encoding an α, α-trehalase of 529 amino acids was cloned from Zunongwangia sp., and TreZ was found to have an optimal activity at 50 °C and pH 6. The activity of TreZ was increased by the presence of NaCl, showing the highest activity (136 %) at 1 M NaCl. A variant C4 with improved catalytic activity was obtained by error-prone PCR and followed by a 96-well plate high-throughput screening. The variant C4 with two altered sites (Y227H, and R442G) displayed a 3.3 fold increase in catalytic efficiency (k cat/K m, 1143.40 mmol(-1) s(-1)) compared with the wild type enzyme (265.91 mmol(-1) s(-1)). In order to explore the contribution of the mutations found in variant C4 to the increased catalytic activity, two mutants Y227H and R442G were constructed by site-directed mutagenesis. The results showed that the catalytic efficiencies of Y227H and R442G were 416.78 mmol(-1) s(-1) and 740.97 mmol(-1) s(-1), respectively, indicating that both mutations contributed to the increased catalytic efficiency of variant C4. The structure modeling and substrate docking revealed that the substitution Y227H enlarged the shape of the binding pocket, to improve the binding of the substrate and the release of the products; while the substitution R442G reduced the size of the side chain and decreased the steric hindrance, which contributed to channel the substrate into the active cavity easier and promote the release of the product. In this study, a novel trehalase was cloned, purified, characterized, and engineered. A variant C4 with dramatically improved catalytic activity was obtained by directed evolution, and the mutation sites Y227H and R442G were found to play a significant role in the catalytic efficiency. The overall results provide useful information about the structure and function of trehalase.

Twitter Demographics

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Mendeley readers

The data shown below were compiled from readership statistics for 14 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 14 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 4 29%
Student > Master 3 21%
Student > Doctoral Student 2 14%
Student > Bachelor 2 14%
Researcher 1 7%
Other 1 7%
Unknown 1 7%
Readers by discipline Count As %
Agricultural and Biological Sciences 5 36%
Biochemistry, Genetics and Molecular Biology 4 29%
Chemistry 2 14%
Immunology and Microbiology 1 7%
Unknown 2 14%

Attention Score in Context

This research output has an Altmetric Attention Score of 4. 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 14 February 2019.
All research outputs
#4,015,924
of 14,860,150 outputs
Outputs from BMC Biotechnology
#264
of 791 outputs
Outputs of similar age
#88,698
of 339,483 outputs
Outputs of similar age from BMC Biotechnology
#1
of 1 outputs
Altmetric has tracked 14,860,150 research outputs across all sources so far. This one has received more attention than most of these and is in the 72nd percentile.
So far Altmetric has tracked 791 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 6.4. 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 339,483 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 73% of its contemporaries.
We're also able to compare this research output to 1 others from the same source and published within six weeks on either side of this one. This one has scored higher than all of them