Mutations derived from a thermophilic polyhydroxyalkanoate 1 synthase ( PhaC ) enhance the thermostability and activity of PhaC 2 from Cupriavidus necator H 16 3 4 5 6
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چکیده
Corresponding author † 14 Short title: Mutations enhancing the thermostability and activity of PHA synthase 15 Department of Marine Biotechnology, National Kaohsiung Marine University 16 Department of Seafood Science, National Kaohsiung Marine University 17 Mailing address: Department of Marine Biotechnology, National Kaohsiung Marine 18 University, No.142, Hai-Chuan Rd., Nan-Tzu Dist. Kaohsiung, Taiwan 19 Tel: +886 7 361 7141 ext. 3815; Fax: +886 7 366 3967 20 E-mail: [email protected] (Der-Shyan Sheu) 21 22 Copyright © 2012, American Society for Microbiology. All Rights Reserved. J. Bacteriol. doi:10.1128/JB.06543-11 JB Accepts, published online ahead of print on 9 March 2012
منابع مشابه
Mutations derived from the thermophilic polyhydroxyalkanoate synthase PhaC enhance the thermostability and activity of PhaC from Cupriavidus necator H16.
The thermophile Cupriavidus sp. strain S-6 accumulated polyhydroxybutyrate (PHB) from glucose at 50°C. A 9.0-kbp EcoRI fragment cloned from the genomic DNA of Cupriavidus sp. S-6 enabled Escherichia coli XL1-Blue to synthesize PHB at 45°C. Nucleotide sequence analysis showed a pha locus in the clone. The thermophilic polyhydroxyalkanoate (PHA) synthase (PhaC(Csp)) shared 81% identity with mesop...
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