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Characterization of a new oxidant-stable serine protease isolated by functional metagenomics

Overview of attention for article published in SpringerPlus, August 2013
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Title
Characterization of a new oxidant-stable serine protease isolated by functional metagenomics
Published in
SpringerPlus, August 2013
DOI 10.1186/2193-1801-2-410
Pubmed ID
Authors

Sophie Biver, Daniel Portetelle, Micheline Vandenbol

Abstract

A novel serine protease gene, SBcas3.3, was identified by functional screening of a forest-soil metagenomic library on agar plates supplemented with AZCL-casein. Overproduction in Escherichia coli revealed that the enzyme is produced as a 770-amino-acid precursor which is processed to a mature protease of ~55 kDa. The latter was purified by affinity chromatography for characterization with the azocasein substrate. The enzyme proved to be an alkaline protease showing maximal activity between pH 9 and 10 and at 50°C. Treatment with the chelating agent ethylenediaminetetraacetic acid irreversibly denatured the protease, whose stability was found to depend strictly on calcium ions. The enzyme appeared relatively resistant to denaturing and reducing agents, and its activity was enhanced in the presence of 10 ml/l nonionic detergent (Tween 20, Tween 80, or Triton X-100). Moreover, SBcas3.3 displayed oxidant stability, a feature particularly sought in the detergent and bleaching industries. SBcas3.3 was activated by hydrogen peroxide at concentrations up to 10 g/l and it still retained 30% of activity in 50 g/l H2O2.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 79 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Brazil 3 4%
Belgium 1 1%
Unknown 75 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 20 25%
Student > Master 17 22%
Researcher 8 10%
Student > Bachelor 7 9%
Student > Doctoral Student 7 9%
Other 12 15%
Unknown 8 10%
Readers by discipline Count As %
Agricultural and Biological Sciences 36 46%
Biochemistry, Genetics and Molecular Biology 21 27%
Immunology and Microbiology 3 4%
Environmental Science 2 3%
Computer Science 1 1%
Other 3 4%
Unknown 13 16%
Attention Score in Context

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 12 September 2013.
All research outputs
#15,279,577
of 22,721,584 outputs
Outputs from SpringerPlus
#932
of 1,852 outputs
Outputs of similar age
#123,594
of 200,084 outputs
Outputs of similar age from SpringerPlus
#46
of 89 outputs
Altmetric has tracked 22,721,584 research outputs across all sources so far. This one is in the 22nd percentile – i.e., 22% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,852 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.7. This one is in the 35th percentile – i.e., 35% 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 200,084 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 28th percentile – i.e., 28% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 89 others from the same source and published within six weeks on either side of this one. This one is in the 10th percentile – i.e., 10% of its contemporaries scored the same or lower than it.