Recombinant production of a shell matrix protein in Escherichia coli and its application to the biomimetic synthesis of spherulitic calcite crystals
SCIE
SCOPUS
- Title
- Recombinant production of a shell matrix protein in Escherichia coli and its application to the biomimetic synthesis of spherulitic calcite crystals
- Authors
- Song, W; Bahn, SY; Cha, HJ; Pack, SP; Choi, YS
- Date Issued
- 2016-05
- Publisher
- SPRINGER
- Abstract
- Objectives To overcome the limited production capability of shell matrix proteins and efficiently conduct in vitro CaCO3 biomineralization studies, a putative recombinant shell matrix protein was prepared and characterized.
Results A glycine-rich protein (GRP_BA) was found in Pinctada fucata as a putative shell matrix protein (NCBI reference sequence; BAA20465). It was genetically redesigned for the production in Escherichia coli. The recombinant protein was obtained in a 400 ml shake-flask culture at approx. 30 mg l(-1) with a purity of > 95 %. It efficiently formed a complex with Ca2+. Ca2+-induced agglomeration was like other calcification-related proteins. Spherulitic calcite micro-particles, 20-30 A mu m diam. with rosette- and sphere-like structures were synthesized in the presence of the recombinant shell protein, which could be formed by stacking and/or aggregation of calcite nanograins and the bound protein.
Conclusions Recombinant production of a shell matrix protein could overcome potential difficulties associated with the limited amount of protein available for biomineralization studies and provide opportunities to fabricate biominerals in practical aspects.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/37647
- DOI
- 10.1007/s10529-016-2039-x
- ISSN
- 0141-5492
- Article Type
- Article
- Citation
- BIOTECHNOLOGY LETTERS, vol. 38, no. 5, page. 809 - 816, 2016-05
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