Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Katsuhisa Saeki"'
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
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1770:716-724
A mutanase (alpha-1,3-glucanase)-producing microorganism was isolated from a soil sample and was identified as a relative of Paenibacillus sp. The mutanase was purified to homogeneity from culture, and its molecular mass was around 57 kDa. The gene f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d55b68d53f38dd94151bc672270163ca
https://doi.org/10.1016/j.bbagen.2006.12.004
https://doi.org/10.1016/j.bbagen.2006.12.004
Autor:
Katsuhisa Saeki, Tohru Kobayashi, Nobuyuki Sumitomo, Susumu Ito, Tsuyoshi Shirai, Yasushi Kageyama
Publikováno v:
World Journal of Microbiology and Biotechnology. 21:961-967
Crystallographic analysis of the highly alkaline M-protease from an alkaliphilic Bacillus strain shows the occurrence of a unique salt bridge triad Arg19–Glu271–Arg275 (in subtilisin BPN′ numbering), which is not found in less alkaline true sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ee9849da3bc18bf7eff46463f7ec58a
https://doi.org/10.1007/s11274-004-7162-5
https://doi.org/10.1007/s11274-004-7162-5
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:
Susumu Ito, Tohru Kobayashi, Marietta V. Magallones, Shuji Kawai, Katsuhisa Saeki, Yasushi Takimura, Yuji Hatada
Publikováno v:
Current Microbiology. 47:337-340
The gene for a new subtilisin from the alkaliphilic Bacillus sp. KSM-LD1 was cloned and sequenced. The open reading frame of the gene encoded a 97 amino-acid prepro-peptide plus a 307 amino-acid mature enzyme that contained a possible catalytic triad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0b442fe5be0b260de64636c078336a3
https://doi.org/10.1007/s00284-002-4018-9
https://doi.org/10.1007/s00284-002-4018-9
Autor:
Kazuaki Igarashi, Katsuhisa Saeki, Hiroshi Hagihara, Katsutoshi Ara, Susumu Ito, Shuji Kawai, Takaaki Uemura, Mikio Takaiwa
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1243:315-324
The novel alkaline amylopullulanase produced by alkalophilic Bacillus sp. KSM-1378 was purified to an electrophoretically homogeneous state from culture medium. The purified enzyme was a glycoprotein with an apparent molecular mass of about 210 kDa a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1687efdf7024e751175695940150de0
https://doi.org/10.1016/0304-4165(94)00148-q
https://doi.org/10.1016/0304-4165(94)00148-q
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 59:662-666
Alkalophilic Bacillus sp. KSM-1378 produces an alkaline amylopullulanase that hydrolyzes both α-1,4 linkages in amylose, amylopectin, and glycogen and α-1,6 linkages in pullulan. The hydrolytic activities against amylose and pullulan were specifica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a413bd69801cd986c1a1a16f8eeeb97
https://doi.org/10.1271/bbb.59.662
https://doi.org/10.1271/bbb.59.662
Publikováno v:
Journal of General Microbiology. 139:781-786
Summary: Alkaline isoamylase (glycogen 6-glucanohydrolase, EC 3.2.1.68) activity was detected in the culture medium of an alkalophilic strain of Bacillus sp., designated KSM-3309, which was isolated from a soil sample. This novel enzyme was purified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0aefa20168c6cc9aa2698a83a38995c6
https://doi.org/10.1099/00221287-139-4-781
https://doi.org/10.1099/00221287-139-4-781
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 56:62-65
A novel alkaline pullulanase (pullulan 6-glucanohydrolase, EC 3.2.1.41) was purified to homogeneity from the culture filtrate of the alkalophilic Bacillus sp. KSM-1876. The pullulanase had an optimum pH for activity of around 10.0–10.5, which is th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a1ddb6c011341885e1e14ec54eecd78
https://doi.org/10.1271/bbb.56.62
https://doi.org/10.1271/bbb.56.62