• Title/Summary/Keyword: GG1234

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In vitro CaCO3 Crystallization at Room Temperature and Atmospheric Pressure Using Recombinant Proteins GRP_BA and GG1234 (재조합단백질 GRP_BA 및 GG1234를 이용한, 상온상압조건에서의 In vitro 탄산칼슘 결정화)

  • Son, Chaeyeon;Song, Wooho;Choi, Hyunsuk;Choi, Yoo Seong
    • Korean Chemical Engineering Research
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    • v.57 no.2
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    • pp.205-209
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    • 2019
  • The exquisite structure and attractive biological properties of biominerals have great potential and increased interest for use in a wide range of medical and industrial applications. Calcium carbonate biomineralization, mainly controlled by shell matrix proteins, has been used as a representative model to understand the biomineralization mechanism. In this study, in vitro calcium carbonate crystallization was carried out under room temperature and atmospheric pressure using recombinant shell matrix protein GRP_BA and artificial shell matrix protein GG1234. Both proteins inhibited the growth of typical rhombohedral calcite crystals in the calcium carbonate crystallization using $CaCl_2$ solution and $(NH_4)_2CO_3$ vapor, and spherulitic calcite crystals with rosette-like structures were synthesized in both the presence of GRP_BA and GG1234. These results might be caused by the properties of block-like domain structure and intrinsically disordered proteins. We expect that this study can contribute to enhance understanding of the calcium carbonate biomineralization controlled by shell matrix proteins.

Production of Recombinant GG1234-DsRed Fusion Protein and Its Effect on in vitro CaCO3 Crystallization (재조합 GG1234-DsRed 융합 단백질의 생산 및 In vitro 탄산칼슘 결정화에 미치는 영향에 대한 연구)

  • Son, Chaeyeon;Kim, Jin Ho;Kim, Ji Ha;Choi, Yoo Seong
    • KSBB Journal
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    • v.30 no.6
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    • pp.296-301
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    • 2015
  • Eggshell-based biocomposites have become attractive due to their exquisite nanostructure and biological properties, which are mainly composed of highly organized calcium carbonate crystals controlled by organic macromolecules such as proteins and polysaccharides. Here, we designed the recombinant fusion protein of a putative eggshell matrix protein named as GG1234 and a fluorescent reporter protein of DsRed. The protein was successfully over-expressed in E. coli and purified by Ni-NTA affinity chromatography. In vitro calcium carbonate crystallization was conducted in the presence of the fusion protein, and morphological change was investigated. The protein inhibited the calcite growth in vitro, and spherical calcium carbonate micro-particles with the diameter of about $20-30{\mu}m$ were obtained. We expect that this study would be helpful for better understanding of eggshell-based biomineralization.