R5 Peptide-based Biosilicification Using Methyltrimethoxysilane

• Published in: Biotechnology and bioprocess engineering Vol. 23; no. 1; pp. 11 - 15
• Main Authors: Park, Jeong Chan, Kim, Do Hyeon, Kim, Chang Sup, Seo, Jeong Hyun
• Format: Journal Article
• Language: English
• Published: Seoul The Korean Society for Biotechnology and Bioengineering 01.02.2018; Springer Nature B.V; 한국생물공학회
• Subjects: Biotechnology; Chemical engineering; Chemistry; Chemistry and Materials Science; Chromatography; Cylindrotheca; E coli; Enzymes; Escherichia coli; Fusion protein; Hydrophobicity; Industrial and Production Engineering; Microscopy; particle size; Peptides; phosphates; Precursors; Proteins; Research Paper; Silicic acid; Tetraethyl orthosilicate; 생물공학; biosilica; methyltrimethoxysilane; hydrophobic silane; GFP-R5 fusion system
• ISSN: 1226-8372; 1976-3816
• DOI: 10.1007/s12257-017-0451-2

We examined the performance of methyltrimethoxysilane (MTMS), a precursor of silicic acid, in the process of biosilicification induced by the R5 peptide from Cylindrotheca fusiformis . Recombinant GFP-R5 fusion protein was produced by Escherichia coli cultured at 25°C as a soluble and functional formation, but not at 37°C. MTMS-based biosilica deposits had a larger average diameter compared to tetraethyl orthosilicate (TEOS)-based deposits. Reducing phosphate concentration in the buffer system led to a decrease in the size of MTMS-based biosilica. These results provide insight into the surface modification of biosilica, and control of biosilica particle size, when using hydrophobic precursors such as MTMS.