Search Results - "TAKEHANA, Toshihiko"

Purification and Characterization of a Liquefying α-Amylase from Alkalophilic Thermophilic Bacillus sp. AAH-31 by KIM, Dae Hoon, MORIMOTO, Naoki, SABURI, Wataru, MUKAI, Atsushi, IMOTO, Koji, TAKEHANA, Toshihiko, KOIKE, Seiji, MORI, Haruhide, MATSUI, Hirokazu

“…α-Amylase (EC 3.2.1.1) hydrolyzes an internal α-1,4-glucosidic linkage of starch and related glucans. Alkalophilic liquefying enzymes from Bacillus species are…”
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A bacterium that degrades and assimilates poly(ethylene terephthalate) by Yoshida, Shosuke, Hiraga, Kazumi, Takehana, Toshihiko, Taniguchi, Ikuo, Yamaji, Hironao, Maeda, Yasuhito, Toyohara, Kiyotsuna, Miyamoto, Kenji, Kimura, Yoshiharu, Oda, Kohei

“…Poly(ethylene terephthalate) (PET) is used extensively worldwide in plastic products, and its accumulation in the environment has become a global concern…”
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Ideonella sakaiensis sp. nov., isolated from a microbial consortium that degrades poly(ethylene terephthalate) by Tanasupawat, Somboon, Takehana, Toshihiko, Yoshida, Shosuke, Hiraga, Kazumi, Oda, Kohei

“…A Gram-stain-negative, aerobic, non-spore-forming, rod-shaped bacterium, designed strain 201-F6T, was isolated from a microbial consortium that degrades…”
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Response to Comment on "A bacterium that degrades and assimilates poly(ethylene terephthalate)" by Yoshida, Shosuke, Hiraga, Kazumi, Takehana, Toshihiko, Taniguchi, Ikuo, Yamaji, Hironao, Maeda, Yasuhito, Toyohara, Kiyotsuna, Miyamoto, Kenji, Kimura, Yoshiharu, Oda, Kohei

“…Yang et al suggest that the use of low-crystallinity poly(ethylene terephthalate) (PET) exaggerates our results. However, the primary focus of our study was…”
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Purification and properties of extracellular carboxyl proteases of acid-tolerant bacteria, isolated from compost by Takehana, T. (Hokkaido Univ., Sapporo (Japan)), Inoue, S, Takei, R, Ito, H, Matsui, H, Honma, M

“…Four strains of acid-tolerant and protein-using bacteria were isolated from compost. Two of them, Gram-negative strains MB8 and MB11, were identified as a new…”
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Enhancement of hydrolytic activity of thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 through optimization of amino acid residues surrounding the substrate binding site by Tamamura, Naoya, Saburi, Wataru, Mukai, Atsushi, Morimoto, Naoki, Takehana, Toshihiko, Koike, Seiji, Matsui, Hirokazu, Mori, Haruhide

“…•AmyL with N-terminal starch binding domain belongs to GH family 13.•AmyL has high tolerance to high temperature, high pH, chelators, and…”
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A Thermophilic Alkalophilic α-Amylase from Bacillus sp. AAH-31 Shows a Novel Domain Organization among Glycoside Hydrolase Family 13 Enzymes by SABURI, Wataru, MORIMOTO, Naoki, MUKAI, Atsushi, KIM, Dae Hoon, TAKEHANA, Toshihiko, KOIKE, Seiji, MATSUI, Hirokazu, MORI, Haruhide

“…α-Amylases (EC 3.2.1.1) hydrolyze internal α-1,4-glucosidic linkages of starch and related glucans. Bacillus sp. AAH-31 produces an alkalophilic thermophilic…”
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A Thermophilic Alkalophilic [alpha]-Amylase from Bacillus sp. AAH-31 Shows a Novel Domain Organization among Glycoside Hydrolase Family 13 Enzymes by SABURI, Wataru, MORIMOTO, Naoki, MUKAI, Atsushi, Hoon KIM, Dae, TAKEHANA, Toshihiko, KOIKE, Seiji, MATSUI, Hirokazu, MORI, Haruhide

“…α-Amylases (EC 3.2.1.1) hydrolyze internal α-1,4-glucosidic linkages of starch and related glucans. Bacillus sp. AAH-31 produces an alkalophilic thermophilic…”
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Purification and Characterization of a Liquefying [alpha]-Amylase from Alkalophilic Thermophilic Bacillus sp. AAH-31 by KIM, Dae Hoon, MORIMOTO, Naoki, SABURI, Wataru, MUKAI, Atsushi, IMOTO, Koji, TAKEHANA, Toshihiko, KOIKE, Seiji, MORI, Haruhide, MATSUI, Hirokazu

“…α-Amylase (EC 3.2.1.1) hydrolyzes an internal α-1,4-glucosidic linkage of starch and related glucans. Alkalophilic liquefying enzymes from Bacillus species are…”
Get full text