Molecular cloning and expression of amylosucrase from highly radiation-resistant Deinococcus radiopugnans
Food Science and Biotechnology, ISSN: 2092-6456, Vol: 23, Issue: 6, Page: 2007-2012
2014
- 24Citations
- 9Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Article Description
Amylosucrase (AS), a glucosyltransferase of the glycoside hydrolase 13 family, does not require a nucleotide-activated sugar as a glucosyl-donor. A gene (drpas) of Deinococcus radiopugnans encoding a putative AS was identified and cloned for characterization. The amino acid sequence revealed that drpas exhibited 76 and 74% identities with AS genes from D. geothermalis and D. radiodurans, respectively. Recombinant DRpAS exhibited AS activities. The ratios of hydrolysis, polymerization, and isomerization reactions were 5.8:82.7:11.5 at 40°C. The DRpAS was highly thermostable and produced more polymerization products than AS from D. radiodurans although the optimum growth temperature of both strains is 30°C.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84918510117&origin=inward; http://dx.doi.org/10.1007/s10068-014-0273-3; http://link.springer.com/10.1007/s10068-014-0273-3; http://link.springer.com/content/pdf/10.1007/s10068-014-0273-3; http://link.springer.com/content/pdf/10.1007/s10068-014-0273-3.pdf; http://link.springer.com/article/10.1007/s10068-014-0273-3/fulltext.html
Springer Science and Business Media LLC
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