Journal
BIOTECHNOLOGY LETTERS
Volume 38, Issue 5, Pages 809-816Publisher
SPRINGER
DOI: 10.1007/s10529-016-2039-x
Keywords
Biomineralization; Calcium carbonate; Pearl oyster; Recombinant protein; Spherulitic calcite crystal
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Funding
- National Research Foundation of Korea
- Ministry of Science, ICT and Future Planning, Korea [NRF-C1ABA001-2011-0029960, NRF-2012R1A1A1003516]
- Marine Biotechnology Program (Marine BioMaterials Research Center)
- Ministry of Oceans and Fisheries, Korea
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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.
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