Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Dararat, Kakizono"'
Autor:
Osamu Mizutani, Dararat Kakizono, Toru Takahashi, Nobuhiko Mukai, Hisashi Fukuda, Osamu Yamada
Publikováno v:
Bioscience, Biotechnology, and Biochemistry.
To reduce the methanol content in sweet potato shochu, we studied the pectin methylesterase genes of the shochu–koji mold Aspergillus luchuensis. We found the following three homologs of pectin methyleseterase in the genome of A. luchuensis: pmeA,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d0ba209fbbc880fcaee4a551d8064fdf
https://doi.org/10.1093/bbb/zbad049
https://doi.org/10.1093/bbb/zbad049
Autor:
Kazuo Masaki, Dararat Kakizono, Nobuhiko Mukai, Kanako Fujihara, Taichi Mizukure, Masaki Okuda
Publikováno v:
Journal of Bioscience and Bioengineering. 130:577-581
Urethanase (EC 3.5.1.75) catalyzes the hydrolysis of ethyl carbamate (EC) to ethanol, carbon dioxide, and ammonia. From our recent study, we expected that an acetamidase encoded by amdS of Aspergillus oryzae may catalyze the degradation of EC because
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96a3e127ac47aba32c8fd67ccacf45a3
https://doi.org/10.1016/j.jbiosc.2020.07.015
https://doi.org/10.1016/j.jbiosc.2020.07.015
Autor:
Kanako Fujihara, Dararat Kakizono, Kazuo Masaki, Tsutomu Fujii, Taichi Mizukure, Nobuhiko Mukai
Publikováno v:
Journal of Bioscience and Bioengineering. 130:115-120
Urethanase (EC 3.5.1.75) is an effective enzyme for removing ethyl carbamate (EC) present in alcoholic beverages. However, urethanase is not well studied and has not yet been developed for practical use. In this study, we report a new urethanase (CPU
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46b0ec373ab03b1b98c60e0bf1580166
https://doi.org/10.1016/j.jbiosc.2020.03.005
https://doi.org/10.1016/j.jbiosc.2020.03.005
Publikováno v:
Bioscience, biotechnology, and biochemistry. 84(1)
High glycosidase-producing strains of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0d9de7af00aa8ff08067dffce141541f
https://pubmed.ncbi.nlm.nih.gov/31566090
https://pubmed.ncbi.nlm.nih.gov/31566090
High glycosidase-producing strains of Aspergillus luchuensis were isolated from 2-deoxyglucose (2-DG) resistant mutants. α-Amylase, exo-α-1,4-glucosidase, β-glucosidase and β-xylosidase activity in the mutants was ~3, ~2, ~4 and ~2.5 times higher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4930b98f970c80783fb94129b455534
Autor:
Sakurako Ichinose, Dararat Kakizono, Katsuya Gomi, Daisuke Shiro, Osamu Mizutani, Takahiro Shintani, Yasumichi Onozaki, Tomoko Shintani, Jun ichi Yokota, Mizuki Tanaka
Publikováno v:
Applied microbiology and biotechnology. 101(6)
Filamentous fungi are often used as cell factories for recombinant protein production because of their ability to secrete large quantities of hydrolytic enzymes. However, even using strong transcriptional promoters, yields of nonfungal proteins are g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::693e186e5417850fe7a9e89ad95c745e
https://pubmed.ncbi.nlm.nih.gov/28064367
https://pubmed.ncbi.nlm.nih.gov/28064367
Filamentous fungi are widely used for the production of homologous and heterologous proteins. Recently, there has been increasing interest in Aspergillus oryzae because of its ability to produce heterologous proteins in solid-state culture. To provid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d73e726e09ae755416d8b956276360d
https://europepmc.org/articles/PMC1472361/
https://europepmc.org/articles/PMC1472361/