Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/95608
標題: Cloning of phaCAB genes from thermophilic Caldimonas manganoxidans in Escherichia coli for poly(3-hydroxybutyrate) (PHB) production
作者: Lin, Ji-Hong
Lee, Ming-Chieh
Sue, You-Sheng
Liu, Yung-Chuan
Li, Si-Yu
李思禹
關鍵字: Caldimonas manganoxidans;Escherichia coli;Molecular weight;Poly(3-hydroxybutyrate) (PHB);phaCAB gene characterization;Acyltransferases;Biosynthetic Pathways;Cloning, Molecular;Comamonadaceae;Escherichia coli;Hydroxybutyrates;Open Reading Frames;Polyesters;Sequence Alignment
出版社: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Project: Applied microbiology and biotechnology, Volume 101, Issue 16, Page(s) 6419-6430.
摘要: 
PHB biosynthesis pathway, consisting of three open reading frames (ORFs) that encode for β-ketothiolase (phaA Cma , 1179 bp), acetoacetyl-CoA reductase (phaB Cma , 738 bp), and PHA synthase (phaC Cma , 1694 bp), of Caldimonas manganoxidans was identified. The functions of PhaA, PhaB, and PhaC were demonstrated by successfully reconstructing PHB biosynthesis pathway of C. manganoxidans in Escherichia coli, where PHB production was confirmed by OD600, gas chromatography, Nile blue stain, and transmission electron microscope (TEM). The protein sequence alignment of PHB synthases revealed that phaC Cma shares at least 60% identity with those of class I PHB synthase. The effects of PhaA, PhaB, and PhaC expression levels on PHB production were investigated. While the overexpression of PhaB is found to be important in recombinant E. coli, performances of PHB production can be quantified as follows: PHB concentration of 16.8 ± 0.6 g/L, yield of 0.28 g/g glucose, content of 74%, productivity of 0.28 g/L/h, and Mw of 1.41 MDa.
URI: http://hdl.handle.net/11455/95608
DOI: 10.1007/s00253-017-8386-2
Appears in Collections:化學工程學系所

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