Author: Poehlein, Anja ; Dürre, Peter ; Schiel-Bengelsdorf, Bettina ; Daniel, Rolf ; Gottschalk, Gerhard ; Bengelsdorf, Frank R. ; Andreesen, Jan R. ; Cebulla, Martin ; Ilg, Marcus M. ; Whited, Gregg

ABSTRACTClostridium aceticum was the first isolated autotrophic acetogen, converting CO 2 plus H 2 or syngas to acetate. Its genome has now been completely sequenced and consists of a 4.2-Mbp chromosome and a small circular plasmid of 5.7 kbp. Sequence analysis revealed major differences from other autotrophic acetogens. C. aceticum contains an Rnf complex for energy conservation (via pumping protons or sodium ions). Such systems have also been found in C. ljungdahlii and Acetobacterium woodii . However, C. aceticum also contains a cytochrome, as does Moorella thermoacetica , which has been proposed to be involved in the generation of a proton gradient. Thus, C. aceticum seems to represent a link between Rnf- and cytochrome-containing autotrophic acetogens. In C. aceticum , however, the cytochrome is probably not involved in an electron transport chain that leads to proton translocation, as no genes for quinone biosynthesis are present in the genome. IMPORTANCE Autotrophic acetogenic bacteria are receiving more and more industrial focus, as CO 2 plus H 2 as well as syngas are interesting new substrates for biotechnological processes. They are both cheap and abundant, and their use, if it results in sustainable products, also leads to reduction of greenhouse gases. Clostridium aceticum can use both gas mixtures, is phylogenetically not closely related to the commonly used species, and may thus become an even more attractive workhorse. In addition, its energy metabolism, which is characterized here, and the ability to synthesize cytochromes might offer new targets for improving the ATP yield by metabolic engineering and thus allow use of C. aceticum for production of compounds by pathways that currently present challenges for energy-limited acetogens.

28 Aug 2015·Journal of Microbiology and BiotechnologyQ4 · ENGINEERING & TECHNOLOGY

Identification and Characterization of a New Alkaline Thermolysin-Like Protease, BtsTLP1, from Bacillus thuringiensis Serovar Sichuansis Strain MC28

Q4 · ENGINEERING & TECHNOLOGY

Article

Author: Zhang, Zhenghong ; Babe, Lilia ; Xie, Zhiyong ; Hao, Helong ; Zou, Zhengzheng ; Goedegebuur, Frits ; Tang, Zhongmei ; Gu, Xiaogang ; Zhang, Keya

Thermolysin and its homologs are a group of metalloproteases that have been widely used in both therapeutic and biotechnological applications. We here report the identification and characterization of a novel thermolysin-like protease, BtsTLP1, from insect pathogen Bacillus thuringiensis serovar Sichuansis strain MC28. BtsTLP1 is extracellularly produced in Bacillus subtilis, and the active protein was purified via successive chromatographic steps. The mature form of BtsTLP1 has a molecule mass of 35.6 kDa as determined by mass spectrometry analyses. The biochemical characterization indicates that BtsTLP1 has an apparent Km value of 1.57 mg/ml for azocasein and is active between 20°C and 80°C. Unlike other reported neutral gram-positive thermolysin homologs with optimal pH around 7, BtsTLP1 exhibits an alkaline pH optimum around 10. The activity of BtsTLP1 is strongly inhibited by EDTA and a group of specific divalent ions, with Zn(2+) and Cu(2+) showing particular effects in promoting the enzyme autolysis. Furthermore, our data also indicate that BtsTLP1 has potential in cleaning applications.

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