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Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp.: cloning, expression and characterization.
Tsutsumi, Gaku; Kuroki, Chikako; Kamei, Kengo; Kusuda, Mizuho; Nakazawa, Masami; Sakamoto, Tatsuji; Ishikawa, Mariko; Harada, Shinji; Kobayashi, Hitoshi; Ouchi, Kenji; Inatomi, Satoshi; Sakaguchi, Minoru; Iwamoto, Takeo; Ueda, Mitsuhiro.
Affiliation
  • Tsutsumi G; a Graduate School of Agriculture, Osaka Metropolitan University.
  • Kuroki C; a Graduate School of Agriculture, Osaka Metropolitan University.
  • Kamei K; a Graduate School of Agriculture, Osaka Metropolitan University.
  • Kusuda M; a Graduate School of Agriculture, Osaka Metropolitan University.
  • Nakazawa M; a Graduate School of Agriculture, Osaka Metropolitan University.
  • Sakamoto T; a Graduate School of Agriculture, Osaka Metropolitan University.
  • Ishikawa M; b Hokuto Corporation, Mushroom Research Laboratory.
  • Harada S; b Hokuto Corporation, Mushroom Research Laboratory.
  • Kobayashi H; b Hokuto Corporation, Mushroom Research Laboratory.
  • Ouchi K; b Hokuto Corporation, Mushroom Research Laboratory.
  • Inatomi S; b Hokuto Corporation, Mushroom Research Laboratory.
  • Sakaguchi M; c Laboratory of Cell Biology, Osaka University of Pharmaceutical Sciences.
  • Iwamoto T; d Core Research Facilities for Basic Science (Molecular Cell Biology), Jikei University School of Medicine.
  • Ueda M; a Graduate School of Agriculture, Osaka Metropolitan University.
Mycoscience ; 63(6): 284-292, 2022.
Article in En | MEDLINE | ID: mdl-37089524
ABSTRACT
The N-terminal amino acid sequence of the Pleurotus sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from P. ostreatus PC 15 v2.0. The length of the Pleurotus sp. trehalase gene was 2247 bp, encoding a protein of 749 amino acids with a predicted molecular mass of 81.2 kDa. The molecular mass of the recombinant enzyme was estimated to be about 117 kDa by SDS-PAGE. We found that the recombinant enzyme comprised an N-glycosylated sugar chain and that its optimum pH and temperature were 4.5 and 40 ºC, respectively. Moreover, this enzyme exhibited high activity against trehalose exclusively. We found that the enzyme is novel acid trehalase belonging to GH family 37.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Mycoscience Year: 2022 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Mycoscience Year: 2022 Document type: Article