Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Mitsuyoshi Okuda"'
Autor:
Takahiro Hioki, Daichi Yamashita, Masatoshi Tohata, Keiji Endo, Akihito Kawahara, Mitsuyoshi Okuda
Publikováno v:
Microbial Cell Factories, Vol 20, Iss 1, Pp 1-13 (2021)
Abstract Background Most of the proteases classified into the M23 family in the MEROPS database exhibit staphylolytic activity and have potential as antibacterial agents. The M23 family is further classified into two subfamilies, M23A and M23B. Prote
Externí odkaz:
https://doaj.org/article/5fa228b4eccc417a9d41a1cf3cfcc0d4
Autor:
Tatsuya Osamura, Mitsuyoshi Okuda, Atsushi Yamaguchi, Kazumasa Ohtake, Kensaku Sakamoto, Yasushi Takimura
Publikováno v:
Biochemistry and Biophysics Reports, Vol 17, Iss , Pp 93-96 (2019)
In the present study, we attempted to control the pH profile of the catalytic activity of the industrially relevant alkaline protease KP-43, by incorporating 3-nitro-l-tyrosine and 3-chloro-l-tyrosine at and near the catalytic site. Thirty KP-43 vari
Externí odkaz:
https://doaj.org/article/2235631b024f4a32a7ffb022c5649ab3
Autor:
Tatsuya Osamura, Kyoshiro Nonaka, Fumikazu Takahashi, Mitsuyoshi Okuda, Hiroshi Hagihara, Yasushi Takimura
Publikováno v:
Journal of Bioscience and Bioengineering. 134:89-94
The present study investigated high-yield monoacylglycerol (MAG) synthesis by bacterial lipolytic enzymes in a solvent-free two-phase system. Esterification by monoacylglycerol lipase from Bacillus sp. H-257 (H257) required a high glycerol/fatty acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65773d3ea29be133faa6ca126e1c1601
https://doi.org/10.1016/j.jbiosc.2022.05.004
https://doi.org/10.1016/j.jbiosc.2022.05.004
Publikováno v:
Applied Microbiology and Biotechnology
Abstract KP-43, a 43-kDa alkaline serine protease, is resistant to chemical oxidants and surfactants, making it suitable for use in laundry detergents. An amino acid residue at position 195, in a unique flexible loop that binds a Ca2+ ion, dramatical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a608d702f17a85f8d016ae36069885d
https://doi.org/10.1007/s00253-020-10826-2
https://doi.org/10.1007/s00253-020-10826-2
Autor:
Mitsuyoshi Okuda, Atsushi Yamaguchi, Kazumasa Ohtake, Kensaku Sakamoto, Yasushi Takimura, Tatsuya Osamura
Publikováno v:
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 17, Iss, Pp 93-96 (2019)
Biochemistry and Biophysics Reports, Vol 17, Iss, Pp 93-96 (2019)
In the present study, we attempted to control the pH profile of the catalytic activity of the industrially relevant alkaline protease KP-43, by incorporating 3-nitro-l-tyrosine and 3-chloro-l-tyrosine at and near the catalytic site. Thirty KP-43 vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeafa7516e71b608e9c5cc68f623da2a
https://pubmed.ncbi.nlm.nih.gov/30582013
https://pubmed.ncbi.nlm.nih.gov/30582013
Autor:
Tadahiro Ozawa, Tsuyoshi Sato, Masatoshi Tohata, Mitsuyoshi Okuda, Katsuhisa Saeki, Katsuya Ozaki
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834:634-641
We improved the enzymatic properties of the oxidatively stable alkaline serine protease KP-43 through protein engineering to make it more suitable for use in laundry detergents. To enhance proteolytic activity, the gene encoding KP-43 was mutagenized
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f205b1e92ada5f47055e908c6055778f
https://doi.org/10.1016/j.bbapap.2012.12.019
https://doi.org/10.1016/j.bbapap.2012.12.019
Autor:
Tohru Kobayashi, Shuji Kawai, Yasushi Takimura, Akinori Ogawa, Mitsuyoshi Okuda, Nobuyuki Sumitomo, Katsuhisa Saeki, Susumu Ito
Publikováno v:
Extremophiles. 8:229-235
Six genes encoding high-molecular-mass subtilisins (HMSs) of alkaliphilic Bacillus spp. were cloned and sequenced. Their open reading frames of 2,394-2,424 bp encoded prosubtilisins of 798-808 amino acids (aa) consisting of the prepropeptides of 151-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dc9817293d88b19f0709ded09cc627c
https://doi.org/10.1007/s00792-004-0381-8
https://doi.org/10.1007/s00792-004-0381-8
Autor:
Katsuhisa Saeki, Susumu Ito, Nobuyuki Sumitomo, Tohru Kobayashi, Mitsuyoshi Okuda, Shuji Kawai, Akinori Ogawa
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1624:109-114
A high-molecular-mass subtilisin was found in culture broth of the alkaliphilic Bacillus sp. strain KSM-KP43. The gene encoding the enzyme (FT protease) was determined using a mixed primer designed from the N-terminal amino acid (aa) sequence of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2775be376618c8e7674b8e954cdd9432
https://doi.org/10.1016/j.bbagen.2003.10.002
https://doi.org/10.1016/j.bbagen.2003.10.002
Autor:
Mitsuo Takano, Saowanit Tongpim, Yoshikatsu Murooka, Hisayo Ono, Atsuhiko Shinmyo, Yoshinobu Kaneko, Ko Imai, Shouhei Sakuda, Mitsuyoshi Okuda
Publikováno v:
Journal of Fermentation and Bioengineering. 85:362-368
A moderately halophilic and halotolerant eubacterium, strain KS3, was isolated from a salty soil in Thailand and identified as Halomonas elongata based on the results of conventional taxonomic and DNA-DNA reassociation studies. H. elongata KS3 grows
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5acebd37bc51ade19acd732c46733f3b
https://doi.org/10.1016/s0922-338x(98)80078-0
https://doi.org/10.1016/s0922-338x(98)80078-0
Autor:
Kazuhiro Saito, Katsuya Ozaki, Yasushi Takimura, Susumu Ito, Yasushi Kageyama, Mitsuyoshi Okuda, Katsuhisa Saeki, Tohru Kobayashi
Publikováno v:
Applied microbiology and biotechnology. 76(2)
The presence of 11 genes encoding subtilisin-like serine proteases was demonstrated by cloning from the genome of alkaliphilic Bacillus sp. strain KSM-LD1. This strain exoproduces the oxidatively stable alkaline protease LD-1 (Saeki et al. Curr Micro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f848de3d98171a6b81906a3905fcc638
https://pubmed.ncbi.nlm.nih.gov/17571258
https://pubmed.ncbi.nlm.nih.gov/17571258