Effect of applied voltage and temperature on methane production and microbial community in microbial electrochemical anaerobic digestion systems treating swine manure.

Microbial electrochemical technology (MET) that can harvest electricity/valuable materials and enhance the efficiency of conventional biological processes through the redox reaction of organic/inorganic compounds has attracted considerable attention. MET-based anaerobic digestion (AD) systems treating swine manure were operated at different applied voltages (0.1, 0.

Pedobacter soyangensis sp. nov., isolated from Lake Soyang in Korea.

Strain HME6451(T) was isolated from Lake Soyang in Korea. Phylogenetic tree based on 16S rRNA gene sequence showed that strain HME6451(T) formed a lineage within the genus Pedobacter. The strain HME6451(T) was closely related to Pedobacter daechungensis (95.

Pontibacter jeungdoensis sp. nov., isolated from a solar saltern in Korea.

A Gram-staining-negative, rod-shaped and red-pigmented bacterial strain, HMD3125(T), was isolated from a solar saltern in Jeungdo, Republic of Korea. A phylogenetic tree based on 16S rRNA gene sequences showed that strain HMD3125(T) formed a lineage within the genus Pontibacter and was similar to Pontibacter salisaro (96.1%) and P.

An enzymatic method to distinguish tetrahydrobiopterin from oxidized biopterins using UDP-glucose:tetrahydrobiopterin glucosyltransferase.

The quantitative determination of tetrahydrobiopterin (BH4) and its oxidized forms (dihydrobiopterin and biopterin) is important in searching for possible markers of neuropsychiatric and cardiovascular disorders as well as in diagnosing BH4 deficiencies. Currently, two high-performance liquid chromatography (HPLC) methods are available, although both have some limitations. We developed an enzymatic method to distinguish BH4 from the oxidized forms by employing BH4:UDP-glucose alpha-glucosyltransferase (BGluT), which catalyzes glucosyl transfer from UDP-glucose to BH4.

6-Pyruvoyltetrahydropterin synthase orthologs of either a single or dual domain structure are responsible for tetrahydrobiopterin synthesis in bacteria.

6-Pyruvoyltetrahydropterin synthase (PTPS) catalyzes the second step of tetrahydrobiopterin (BH4) synthesis. We previously identified PTPS orthologs (bPTPS-Is) in bacteria which do not produce BH4. In this study we disrupted the gene encoding bPTPS-I in Synechococcus sp.