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Electrochemical characterization of a unique, "neutral" laccase from Flammulina velutipes
http://hdl.handle.net/2297/33410
http://hdl.handle.net/2297/33410a1b3e7ef-124d-45a4-9fb5-a9ec5e6320f2
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SC-PR-SAKURAI-T-159.pdf (1.0 MB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-03 | |||||
| タイトル | ||||||
| タイトル | Electrochemical characterization of a unique, "neutral" laccase from Flammulina velutipes | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Saito-Otsuka, Kaori
× Saito-Otsuka, Kaori× Kurose, Shinji× Tsujino, Yoshio× Osakai, Toshiyuki× Kataoka, Kunishige× Sakurai, Takeshi× Tamiya, Eiichi |
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| 書誌情報 |
Journal of Bioscience and Bioengineering 巻 115, 号 2, p. 159-167, 発行日 2013-02-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 1389-1723 | |||||
| NCID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA11307678 | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1016/j.jbiosc.2012.09.011 | |||||
| 出版者 | ||||||
| 出版者 | Society for Biotechnology, Japan (日本生物工学会) / Elsevier | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The flac1 gene consisted of 1488 bases encodes a novel laccase (Flac1) from Flammulina velutipes. The deduced amino acid sequence of Flac1 with 496 amino acids shows 58-64% homologies with other fungal laccases. The recombinant Flac1 (rFlac1) was heterologously expressed in Pichia pastoris, with sugars of approximately 4 kDa attached on the protein molecule, which has the calculated molecular mass of 53,532 Da. rFlac1 was shown to be a multi-copper oxidase from spectroscopies. The optimum pHs of rFlac1 for oxidations of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), p-phenylenediamine, and o-aminophenol, were 5.0, 5.0, and 6.0-6.5, respectively, showing higher pH values than those from many other fungal laccases. The slightly acidic or neutral optimum pH that is not strongly dependent on substrates is a unique property of rFlac1. Effective O2 reduction was realized by the direct electron transfer of rFlac1 at a highly oriented pyrolytic graphite electrode modified with fine carbon particles (Ketjen Black) in O2-saturated solution. The pHs showing the maximum ΔE°' [= E°'(enzyme) - E°'(substrate)] coincided well with the optimum pHs shown by rFlac1 under steady-state conditions. The present electrochemical results of rFlac1 indicate that ΔE°' is one of the primary factors to determine the activity of multi-copper oxidases. © 2012 The Society for Biotechnology, Japan | |||||
| 著者版フラグ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
