Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Yusaku MATSUMOTO"'
Publikováno v:
Journal of Advanced Mechanical Design, Systems, and Manufacturing, Vol 13, Iss 5, Pp JAMDSM0097-JAMDSM0097 (2019)
The agricultural sector is required to produce a steady, year-round supply of crops to maintain the quality of life of consumers. The organization of agricultural production has, therefore, become increasingly important. This study aims to evaluate t
Externí odkaz:
https://doaj.org/article/3205980103ff4dc6a5712371c434f9c0
Publikováno v:
Nihon Kikai Gakkai ronbunshu, Vol 85, Iss 872, Pp 18-00148-18-00148 (2019)
It is becoming necessary for agriculture companies to deal with daily stable supplies for farm produces because customers who hope to achieve quality of life (QOL) in daily meal are getting increasing. Therefore, it is increasingly important to resea
Externí odkaz:
https://doaj.org/article/350c46d38b304ba186ef3d131039d10b
Autor:
Yusaku Matsumoto1, Hayato Kizaki1, Yuki Ikeda2, Shohei Nakamura3, Shinya Kina3, Takanori Nagai2, Takafumi Nasu2, Koji Miyamoto2, Satoko Hori1
Publikováno v:
Drug Discoveries & Therapeutics. Dec2021, Vol. 15 Issue 6, p337-340. 4p.
Autor:
Ikuhide Fujisawa, Yusaku Matsumoto, Kazutaka Murayama, Daisuke Sugimori, Hiroaki Hamana, Yu Tomita
Publikováno v:
Journal of bioscience and bioengineering. 131(1)
Sphingomyelinase C (SMC) hydrolyzes sphingomyelin to ceramide and phosphocholine. Prokaryotic SMCs share sequence homology with mammalian SMCs that have enzymatic pH optima at neutral pH. SMC from the nonpathogenic prokaryote Streptomyces griseocarne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48ea1fd09ec22df61c19fe1258ea6423
https://pubmed.ncbi.nlm.nih.gov/33023861
https://pubmed.ncbi.nlm.nih.gov/33023861
Autor:
Yusaku Matsumoto, Daisuke Sugimori, Kazutaka Murayama, Shin ich Sakasegawa, Hideyuki Matsumoto, Takayuki Oyama, Nana Kashiwabara
Publikováno v:
FEBS Open Bio
Lysoplasmalogen (LyPls)-specific phospholipase D (LyPls-PLD) is an enzyme that catalyses the hydrolytic cleavage of the phosphoester bond of LyPls, releasing ethanolamine or choline, and 1-(1-alkenyl)-sn-glycero-3-phosphate (lysoplasmenic acid). Litt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a41fe98b601c01694ec4ac3aad722641
https://doi.org/10.1002/2211-5463.12131
https://doi.org/10.1002/2211-5463.12131
Autor:
Yusaku Matsumoto, Daisuke Sugimori
Publikováno v:
Journal of Bioscience and Bioengineering. 120:372-379
The substrate recognition mechanism of phospholipase D and enzymatic measurement of choline plasmalogen were investigated. A phospholipase D (PLD684) from Streptomyces sp. strain NA684 was purified 184-fold from the culture supernatant with 23.7% rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5f4110431b74b3e1ca0ec242e817e90
https://doi.org/10.1016/j.jbiosc.2015.02.020
https://doi.org/10.1016/j.jbiosc.2015.02.020
Publikováno v:
2017 IEEE International Conference on Industrial Engineering and Engineering Management (IEEM).
A stable continuous supply of products is required to improve consumers' quality of life; thus, the development of agricultural production systems has become critically important. In agriculture (cultivated fields), goods disposals or shortages can r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd93cc22341871b28e0c1968946b2c3d
https://doi.org/10.1109/ieem.2017.8289911
https://doi.org/10.1109/ieem.2017.8289911
Publikováno v:
FEBS Open Bio
A novel metal ion-independent phospholipase A1 of Streptomyces albidoflavus isolated from Japanese soil has been purified and characterized. The enzyme consists of a 33-residue N-terminal signal secretion sequence and a 269-residue mature protein wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3553662466fb41f8fc9a2ea2303be2a4
https://doi.org/10.1016/j.fob.2012.09.006
https://doi.org/10.1016/j.fob.2012.09.006
Publikováno v:
Journal of Advanced Mechanical Design, Systems, and Manufacturing. 13:JAMDSM0097-JAMDSM0097
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eeb25f8d8036fc77e3aff42deba7d5f5
https://doi.org/10.1299/jamdsm.2019jamdsm0097
https://doi.org/10.1299/jamdsm.2019jamdsm0097
Publikováno v:
Biotechnology Letters. 33:727-731
The structural gene for sphingomyelinase (SMase) from Streptomyces griseocarneus, was introduced into Streptomyces lividans using a shuttle vector, pUC702, for Escherichia coli/S. lividans. High-level secretory production of SMase was achieved using
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad56e2890d5ea6a27ebb139a5afa7bb4
https://doi.org/10.1007/s10529-010-0480-9
https://doi.org/10.1007/s10529-010-0480-9