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RESEARCH PRODUCT
Nucleation and Growth of CaCO3 Mediated by the Egg-White Protein Ovalbumin: A Time-Resolved in situ Study Using Small-Angle Neutron Scattering
Wolfgang TremelStephan E. WolfMathias BalzDietmar SchwahnVitaliy Pipichsubject
Protein FoldingOvalbuminProtein ConformationChemistryNeutron diffractionNucleationWaterGeneral ChemistryNeutron scatteringBiochemistrySmall-angle neutron scatteringCatalysisCalcium Carbonatelaw.inventionAmorphous solidCalcium ChlorideNeutron DiffractionCrystallographyColloid and Surface ChemistrylawVateriteScattering Small AngleCrystallizationCrystallizationDissolutiondescription
Mineralization of calcium carbonate in aqueous solutions starting from its initiation was studied by time-resolved small-angle neutron scattering (SANS). SANS revealed that homogeneous crystallization of CaCO 3 involves an initial formation of thin plate-shaped nuclei which subsequently reassemble to 3-dimensional particles, first of fractal and finally of compact structure. The presence of the egg-white protein ovalbumin leads to a different progression of mineralization through several stages; the first step represents amorphous CaCO 3, whereas the other phases are crystalline. The formation and dissolution of the amorphous phase is accompanied by Ca (2+)-mediated unfolding and cross-linking of about 50 protein monomers showing the characteristic scattering of linear chains with a large statistical segment length. The protein complexes act as nucleation centers for the amorphous phase because of their enrichment by Ca (2+) ions. SANS revealed the sequential formation of CaCO 3 starting from the amorphous phase and the subsequent formation of the crystalline polymorphs vaterite and aragonite. This formation from less dense to more dense polymorphs follows the Ostwald-Volmer rule.
year | journal | country | edition | language |
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2008-05-01 | Journal of the American Chemical Society |