Degradation mechanism of tin phosphide as Na-ion battery negative electrode

The degradation mechanism of an Sn4P3 electrode as Na-ion battery anode was investigated by using a transmission electron microscopic observation. At the first desodiation, we confirmed that Sn nanoparticles with 6 nm in size were dispersed in an amorphous-like P matrix. Compared to this, we observed aggregated Sn particles with sizes exceeding 50 nm after the drastic capacity fading. The capacity fading mechanism was for the first time confirmed to be Sn aggregation. To improve the capacity decay, we carried out the two kinds of charge−discharge cycling tests under the reduced volume changes of Sn particles and P matrix by limiting desodiation reactions of NaSn and Na3P, respectively. The Sn4P3 electrode exhibited an excellent cyclability with the discharge capacity of 500 mA h g−1 for 420 cycles under the limited desodiation, whereas the capacity decay was accelerated under the limited sodiation. The results suggest that the Sn aggregation can be improved by the reduced volume change of the P matrix, and that it is very effective for improving anode performance of Sn4P3 electrode

Enhanced Performance of Sn4P3 Electrode Cycled in Ionic Liquid Electrolyte at Intermediate Temperature as Na‐Ion Battery Anode

Charge-discharge performances of Sn4P3 anodes for Na‐ion battery were evaluated in an ionic liquid electrolyte using N‐methyl‐N‐propylpyrrolidinium bis(fluorosulfonyl)amide at intermediate temperatures of 60 and 90 oC. At these temperatures, the anode showed extra capacities based on the full sodiation of Sn in a potential range below 0.2 V vs. Na+/Na because its slow kinetics was improved by elevating operation temperature. Under the current density of 0.1 A g-1 (0.08 C), the Sn4P3 anode at 60 oC exhibited a large capacity of 750 mA h g-1 at the 120th cycle and high Coulombic efficiencies above 99% after the 5th cycle. On the other hand, the efficiency degraded at 90 oC by the electrolyte decomposition. At 60 oC, the anode attained an excellent rate performance with capacity of 250 mA h g-1 even at 3 A g-1 (2.65 C). These results demonstrated the promising operation at intermediate temperature at around 60 oC for Sn4P3 anode in ionic liquid electrolyte

Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA

To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science

Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-N2-) Methyltransferase (Trm11-Trm112 Complex)

The Saccharomyces cerevisiae Trm11 and Trm112 complex (Trm11-Trm112) methylates the 2-amino group of guanosine at position 10 in tRNA and forms N2-methylguanosine. To determine the elements required in tRNA for methylation by Trm11-Trm112, we prepared 60 tRNA transcript variants and tested them for methylation by Trm11-Trm112. The results show that the precursor tRNA is not a substrate for Trm11-Trm112. Furthermore, the CCA terminus is essential for methylation by Trm11-Trm112, and Trm11-Trm112 also only methylates tRNAs with a regular-size variable region. In addition, the G10-C25 base pair is required for methylation by Trm11-Trm112. The data also demonstrated that Trm11-Trm112 recognizes the anticodon-loop and that U38 in tRNAAla acts negatively in terms of methylation. Likewise, the U32-A38 base pair in tRNACys negatively affects methylation. The only exception in our in vitro study was tRNAValAAC1. Our experiments showed that the tRNAValAAC1 transcript was slowly methylated by Trm11-Trm112. However, position 10 in this tRNA was reported to be unmodified G. We purified tRNAValAAC1 from wild-type and trm11 gene deletion strains and confirmed that a portion of tRNAValAAC1 is methylated by Trm11-Trm112 in S. cerevisiae. Thus, our study explains the m2G10 modification pattern of all S. cerevisiae class I tRNAs and elucidates the Trm11-Trm112 binding sites

Prevalence and antimicrobial resistance of Enterococcus spp. isolated from animal feed in Japan

The rising prevalence of antimicrobial resistance (AMR) of bacteria is a global health problem at the human, animal, and environmental interfaces, which necessitates the “One Health” approach. AMR of bacteria in animal feed are a potential cause of the prevalence in livestock; however, the role remains unclear. To date, there is limited research on AMR of bacteria in animal feed in Japan. In this study, a total of 57 complete feed samples and 275 feed ingredient samples were collected between 2018 and 2020. Enterococcus spp. were present in 82.5% of complete feed (47/57 samples), 76.5% of soybean meal (62/81), 49.6% of fish meal (55/111), 33.3% of poultry meal (22/66), and 47.1% of meat and bone meal (8/17) samples. Of 295 isolates, E. faecium (33.2% of total isolates) was the dominant Enterococcus spp., followed by E. faecalis (14.2%), E. hirae (6.4%), E. durans (2.7%), E. casseliflavus (2.4%), and E. gallinarum (1.0%). Of 134 isolates which were tested for antimicrobial susceptibility, resistance to kanamycin was the highest (26.1%), followed by erythromycin (24.6%), tetracycline (6.0%), lincomycin (2.2%), tylosin (1.5%), gentamicin (0.8%), and ciprofloxacin (0.8%). All Enterococcus spp. exhibited susceptibility to ampicillin, vancomycin, and chloramphenicol. Of 33 erythromycin-resistant isolates, only two showed a high minimum inhibitory concentration value (>128 μg/mL) and possessed ermB. These results revealed that overall resistance to antimicrobials is relatively low; however, animal feed is a source of Enterococcus spp. It is essential to elucidate the causative factors related to the prevalence of AMR in animal feed

Laughter and humor as complementary and alternative medicines for dementia patients

<p>Abstract</p> <p>Background</p> <p>The number of dementia patients has increased worldwide, with an estimated 13.7 million dementia patients in the Asia Pacific region alone. This number is expected to increase to 64.6 million by the year 2050.</p> <p>Discussion</p> <p>As a result of advances in research, there several pharmacological therapies available for the treatment of dementia patients. However, current treatments do not suppress the disease process and cannot prevent dementia, and it will be some time before these goals are realized. In the meantime, complementary and alternative medicine (CAM) is an important aspect in the treatment of dementia patients to improve their quality of life throughout the long course of the disease. Considering the individuality of dementia patients, applicability of laughter and humor therapy is discussed. Even though there are many things that need to be elucidated regarding the mechanisms underlying the beneficial effects of laughter and humor, both may be good CAM for dementia patients if they are applied carefully and properly.</p> <p>Summary</p> <p>In this debate article, the physiological basis and actual application of laughter and humor in the treatment of dementia patients are presented for discussion on the applicability to dementia patients.</p

Degradation mechanism of tin phosphide as Na-ion battery negative electrode

The degradation mechanism of an Sn4P3 electrode as Na-ion battery anode was investigated by using a transmission electron microscopic observation. At the first desodiation, we confirmed that Sn nanoparticles with 6 nm in size were dispersed in an amorphous-like P matrix. Compared to this, we observed aggregated Sn particles with sizes exceeding 50 nm after the drastic capacity fading. The capacity fading mechanism was for the first time confirmed to be Sn aggregation. To improve the capacity decay, we carried out the two kinds of charge−discharge cycling tests under the reduced volume changes of Sn particles and P matrix by limiting desodiation reactions of NaSn and Na3P, respectively. The Sn4P3 electrode exhibited an excellent cyclability with the discharge capacity of 500 mA h g−1 for 420 cycles under the limited desodiation, whereas the capacity decay was accelerated under the limited sodiation. The results suggest that the Sn aggregation can be improved by the reduced volume change of the P matrix, and that it is very effective for improving anode performance of Sn4P3 electrode. Keywords: Tin phosphide (Sn4P3), Ionic liquid electrolyte, Na-ion battery, Negative electrode material, Nanostructur

Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA

To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science