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Yoshitaka Ishii
Researcher at Waseda University
Publications - 43
Citations - 1567
Yoshitaka Ishii is an academic researcher from Waseda University. The author has contributed to research in topics: Dibenzothiophene & Sulfur. The author has an hindex of 22, co-authored 42 publications receiving 1493 citations.
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Journal ArticleDOI
Thermophilic carbon-sulfur-bond-targeted biodesulfurization.
TL;DR: Two bacterial strains, which have been identified as Paenibacilli strains and which are capable of efficiently cleaving carbon-sulfur (C--S) bonds in DBT at high temperatures, have been isolated for the first time.
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Biodesulfurization of dibenzothiophene and its derivatives through the selective cleavage of carbon-sulfur bonds by a moderately thermophilic bacterium Bacillus subtilis WU-S2B.
TL;DR: B. subtilis WU-S2B is considered to have more beneficial properties than other desulfurizing bacteria such as Rhodococcus strains previously reported, particularly from the viewpoint of its capacity for thermophilic desulforization through the CS bond cleavage.
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Improvement of desulfurization activity in Rhodococcus erythropolis KA2-5-1 by genetic engineering.
TL;DR: Rhodococus erythropolis KA2-5-1 can desulfurize dibenzothiophene (DBT) into 2-hydroxybiphenyl and the transformant showed improved desulforization activity for light gas oil (LGO), and sulfur components in LGO before and after the reaction were analyzed with gas chromatography-atomic emission detection.
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Desulfurization of alkylated forms of both dibenzothiophene and benzothiophene by a single bacterial strain.
Morio Kobayashi,Toshimitsu Onaka,Yoshitaka Ishii,Jin Konishi,Mikihiro Takaki,Hideki Okada,Yoshinori Ohta,Kenichi Koizumi,Masanori Suzuki +8 more
TL;DR: The purified monooxygenase, encoded by dszC of KA2-5-1, converted benzothiophene and dibenzothiophenes into benzothsiophene sulfone and diphenyl sulfone, respectively, with the aid of an NADH-dependent oxidoreductase.
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Operon structure and functional analysis of the genes encoding thermophilic desulfurizing enzymes of Paenibacillus sp. A11-2.
TL;DR: In vivo and in vitro exhibition of desulfurization activity of the recombinant genes derived from a Paenibacillus indicates that an E. coli oxidoreductase can be functionally coupled with the monooxygenases of a gram-positive thermophile.