Heterologous expression of LamA gene encoded endo-β-1,3-glucanase and CO2 fixation by bioengineered Synechococcus sp. PCC 7002
| Autor: | Jan-Hendrik Hehemann, Dusko Posarac, Heli Wang, Swati Yewalkar, Francis E. Nano, Xiaotao Bi, Layne A. Woodfin, Sheldon J.B. Duff, Di Li, Sheila Potter |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
biology Mutant Photobioreactor Biomass 010501 environmental sciences Glucanase biology.organism_classification 01 natural sciences Enzyme assay law.invention Microbiology 03 medical and health sciences 030104 developmental biology Biochemistry law Thermotoga maritima Recombinant DNA biology.protein Heterologous expression 0105 earth and related environmental sciences General Environmental Science |
| Zdroj: | Frontiers of Environmental Science & Engineering. 11 |
| ISSN: | 2095-221X 2095-2201 |
| DOI: | 10.1007/s11783-017-0910-1 |
| Popis: | The gene for the catalytic domain of thermostable endo-β-1,3-glucanase (laminarinase) LamA was cloned from Thermotoga maritima MSB8 and heterologously expressed in a bioengineered Synechococcus sp. PCC 7002. The mutant strain was cultured in a photobioreactor to assess biomass yield, recombinant laminarinase activity, and CO2 uptake. The maximum enzyme activity was observed at a pH of 8.0 and a temperature of 70°C. At a CO2 concentration of 5%, we obtained a maximum specific growth rate of 0.083 h–1, a biomass productivity of 0.42 g∙L–1∙d–1, a biomass concentration of 3.697 g∙L–1, and a specific enzyme activity of the mutant strain of 4.325 U∙mg–1 dry mass. All parameters decreased as CO2 concentration increased from 5% to 10% and further to 15% CO2, except enzyme activity, which increased from 5% to 10% CO2. However, the mutant culture still grew at 15% CO2 concentration, as reflected by the biomass productivity (0.26 g∙L–1∙d–1), biomass concentration (2.416 g∙L–1), and specific enzyme activity (3.247 U∙mg–1 dry mass). |
| Databáze: | OpenAIRE |
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