Solubilization and aggregation control of silica-polymerizing enzyme fused with a removable soluble protein

Hidetoshi Oguri, Kazunori Nakashima*, Kasun Godigamuwa, Junnosuke Okamoto, Yudai Takeda, Fumiyoshi Okazaki, Masafumi Sakono, Satoru Kawasaki

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

8 被引用数 (Scopus)

抄録

Silicatein, a silica-polymerizing enzyme, is an attractive and promising biocatalyst in many applications such as the synthesis of bio-functionalized inorganic materials under mild conditions. However, its unfavorable aggregation in aqueous media due to its intermolecular hydrophobic interactions causes difficulties in handling and applications. This study aimed to enhance the solubility of silicatein via fusion with a small soluble protein, ProS2. ProS2-Sil showed high solubility and stability in aqueous media for more than 24 h. The aggregation property of ProS2-silicatein fusion protein (ProS2-Sil) was investigated with and without cleavage of ProS2 tag by site-specific protease. When ProS2 tag was removed, silicatein became aggregated, which was analyzed by transmission electron microscope and fluorescence microscope. ProS2-Sil and mature silicatein showed similar activities in silica polymerization. The present approach allows the utilization of silicatein in the fabrication of novel and functional inorganic biohybrid materials.

本文言語英語
ページ(範囲)222-228
ページ数7
ジャーナルJournal of Bioscience and Bioengineering
133
3
DOI
出版ステータス出版済み - 2022/03

ASJC Scopus 主題領域

  • バイオテクノロジー
  • バイオエンジニアリング
  • 応用微生物学とバイオテクノロジー

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