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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)222-228
Number of pages7
JournalJournal of Bioscience and Bioengineering
Volume133
Issue number3
DOIs
StatePublished - 2022/03

Keywords

  • Biohybrid materials
  • Biosilica
  • Protein aggregation
  • Silica polymerizing enzyme

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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