Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Daisuke Mitsuya"'
Autor:
Manao Ozawa, Hitoshi Abo, Mayumi Kijima, Mariko Uchiyama, Daisuke Mitsuya, Michiko Kawanishi, Ryoji Koike
Publikováno v:
J Vet Diagn Invest
We analyzed the correlation between minimum inhibitory concentrations (MICs) of antimicrobials used in humans and those used in animals to enable comparison of antimicrobial susceptibility between Escherichia coli isolated from humans and those from
Autor:
Masahiko Okai, Daisuke Mitsuya, Yu Wang, Naoto Urano, Masami Ishida, Takuya Hayashi, Mami Tanaka
Publikováno v:
Journal of bioscience and bioengineering. 124(1):43-46
The Yukawa River is an extremely acidic river whose waters on the east foot of the Kusatu-Shirane Volcano (in Gunma Prefecture, Japan) contain sulfate ions. Here we isolated many acid-tolerant yeasts from the Yukawa River, and some of them neutralize
Autor:
Akira Inoue, Daisuke Mitsuya, Masashi Yamamoto, Naoto Urano, Takao Ojima, Masahiko Okai, Tomohiro Suzuki
Publikováno v:
Advances in Microbiology. :387-403
We isolated a novel laminarinase ULam111 from Flavobacterium sp. strain UMI-01. Purified ULam111 showed degradation activity against laminarin with the specific activity of 224 ± 18 U/mg at 30°C and pH 6.0. Its optimum temperature was 50°C, and de
Autor:
Masami Ishida, Naoto Urano, Masahiko Okai, Takuya Sugiyama, Shuo Zhang, Daisuke Mitsuya, Yo Takeuchi
Publikováno v:
Journal of bioscience and bioengineering. 126(2)
We isolated a laminarin-degrading cold-adapted bacterium strain LA from coastal seawater in Sagami Bay, Japan and identified it as a Pseudoalteromonas species. We named the extracellular laminarinase LA-Lam, and purified and characterized it. LA-Lam
Autor:
Nobuo Obara, Shintaro Nagaoka, Masahiko Okai, Naoto Urano, Ayako Kurihara, Masami Ishida, Chisato Suwa, Daisuke Mitsuya
We isolated Cryptococcus sp. T1 from Lake Tazawa’s acidic water in Japan. Cryptococcus sp. T1 neutralized an acidic casamino acid solution (pH 3.0) and released ammonia from the casamino acids to aid the neutralization. The neutralization volume wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::567226fe927099afd2b2377a9a38be74
Autor:
Masami Ishida, Naoto Urano, Daisuke Mitsuya, Kyoko Ogasahara, Michiyo Takehira, Hiroyoshi Matsumura, Shun-ichi Tanaka, Kazufumi Takano, Katsuhide Yutani
Publikováno v:
The Journal of Biochemistry. 155:73-82
To investigate the molecular basis of cold adaptation of enzymes, we determined the crystal structure of the tryptophan synthase α subunit (SfTSA) from the psychrophile Shewanella frigidimarina K14-2 by X-ray analysis at 2.6-Å resolution and also e