Citeromyces matritensis M37 is a salt-tolerant yeast that produces ethanol from salted algae.

Algae are referred to as a third-generation biomass for ethanol production. However, salinity treatment is a problem that needs to be solved, because algal hydrolysates often contain high salt. Here, we isolated the salt-tolerant ethanol-producing yeast Citeromyces matritensis M37 from the east coast of Miura Peninsula in Japan. This yeast grew under osmotic stress conditions (20% NaCl or 60% glucose). It produced 6.55 g/L ethanol from YPD medium containing 15% NaCl after 48 h, and the ethanol accumulation was observed even at 20% NaCl. Using salted Undaria pinnatifida (wakame), we obtained 6.33 g/L glucose from approx. 150 g/L of the salted wakame powder with acidic and heat pretreatment followed by enzymatic saccharification, and the ethanol production reached 2.58 g/L for C. matritensis M37. The ethanol concentration was 1.4 times higher compared with that using the salt-tolerant ethanol-producing yeast Zygosaccharomyces rouxii S11.

Purification of hepatitis C virus core protein in non-denaturing condition.

Hepatitis C virus (HCV) is the major cause of chronic hepatitis and hepatocellular carcinoma. Among its structural proteins, the HCV core protein has been implicated in liver disease. Understanding the role of HCV core proteins in viral diseases is crucial to elucidating disease mechanisms and identifying potential drug targets. However, purification challenges hinder the comprehensive elucidation of the structure and biochemical properties of HCV core proteins. In this study, we successfully solubilized bacterially expressed core protein using a high-salt and detergent-containing buffer and bypassed the denaturing-refolding process. Size-exclusion chromatography revealed three distinct peaks in the HCV-infected cell lysate, with the bacterially expressed soluble core protein corresponding to its second peak. Using a combination of affinity, size exclusion, and multi-modal chromatography purification techniques, we achieved a purity of > 95% for the core protein. Analytical ultracentrifugation revealed monomer formation in the solution. Far UV Circular dichroism spectroscopy identified 25.53% alpha helices and 20.26% beta sheets. These findings strongly suggest that the purified core proteins retained one of the native structures observed in HCV-infected cells.

Removal performance and microbial communities in a sequencing batch reactor treating hypersaline phenol-laden wastewater.

Hypersaline phenol-rich wastewater is hard to be treated by traditional biological systems. In this work, a sequencing batch reactor was used to remove phenol from hypersaline wastewater. The removal performance was evaluated in response to the variations of operating parameters and the microbial diversity was investigated by 454 pyrosequencing. The results showed that the bioreactor had high removal efficiency of phenol and was able to keep stable with the increase of initial phenol concentration. DO, pH, and salinity also affected the phenol removal rate. The most abundant bacterial group was phylum Proteobacteria in the two working conditions, and class Gammaproteobacteria as well as Alphaproteobacteria was predominant subgroup. The abundance of bacterial clusters was notably different along with the variation of operation conditions, resulting in changes of phenol degradation rates. The high removal efficiency of phenol suggested that the reactor might be promising in treating phenol-laden industrial wastewater in high-salt condition.