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Taghreed Elkasaby,Dao Duy Hanh,Hideo Kawaguchi,Masakazu Toyoshima,Akihiko Kondo,Chiaki Ogino 한국생물공학회 2023 Biotechnology and Bioprocess Engineering Vol.28 No.5
For growth and energy, Corynebacterium glutamicum has the ability to assimilate numerous carbon sources in the form of either single or combined substrates. During the growth of C. glutamicum on substrate mixtures, it has shown the ability to co-metabolize the majority of these carbon sources and displays monophasic growth, unlike other microorganisms such as Escherichia coli and Bacillus subtilis, which exhibit either diauxic or biphasic growth. Here, a recombinant strain of C. glutamicum ATCC 13032 was selected for the use in the production of itaconic acid (IA), which is a promising biochemical building block that could be an alternative material for polymer synthesis. For this purpose, an engineered C. glutamicum ATCC 13032 pCH-cadAopt was constructed by introducing the plasmid pCH-cadAopt, which expressed a cis-aconitate dehydrogenase gene (cadA) that originated from Aspergillus terreus. The production of IA was evaluated using a combined mixture of maltose and sodium acetate. The monophasic growth of C. glutamicum in the presence of maltose and sodium acetate was observed and showed final IA titer of 12.63 g/L, and a molar yield of 0.38 mol/mol after 240 h of cultivation. The present study suggests the possibility of utilizing a mixture of carbon sources by C. glutamicum to improve IA production.
( Won Kyung Hong ),( Sun Yeon Heo ),( Hye Mi Park ),( Chul Ho Kim ),( Jung Hoon Sohn ),( Akihiko Kondo ),( Jeong Woo Seo ) 한국미생물 · 생명공학회 2013 Journal of microbiology and biotechnology Vol.23 No.6
The gene encoding squalene synthase (SQS) of the lipidproducing heterotrophic microalga Aurantiochytrium sp. KRS101 was cloned and characterized. The krsSQS gene is 1,551 bp in length and has two exons and one intron. The open reading frame of the gene is 1,164 bp in length, yielding a polypeptide of 387 predicted amino acid residues with a molecular mass of 42.7 kDa. The deduced krsSQS sequence shares at least four conserved regions known to be required for SQS enzymatic activity in other species. The protein, tagged with His6, was expressed into soluble form in Escherichia coli. The purified protein catalyzed the conversion of farnesyl diphosphate to squalene in the presence of NADPH and Mg2+. This is the first report on the characterization of an SQS from a Thraustochytrid microalga.