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Effect of high pressure treatment on ovotransferrin.

Food chemistry (2012-09-18)
Alexandra Acero-Lopez, Aman Ullah, Marina Offengenden, Stephanie Jung, Jianping Wu
RESUMEN

High pressure processing of ovotransferrin was carried out to study the structural and physiochemical changes of ovotransferrin under various pressure levels. At pH 8 and pressures higher than 200 MPa, a decrease in total sulfhydryl groups and an increase in surface hydrophobicity were observed along with a partial aggregation. A gradual shift of denaturation peak towards higher temperature was noticed up to 500 MPa, leading to a total loss of the enthalpy of denaturation at pressures of 600 and 700 MPa, where a significant decrease in intrinsic fluorescence was also observed. At pH 3, the ovotransferrin adopted a molten globule state, associated with a significant increase in surface hydrophobicity and reactive sulfhydryl content; structurally, no clear denaturation peaks in differential scanning calorimetry (DSC) were detected at any level of pressure treatment whereas a noticeable decrease in intrinsic fluorescence was evidenced up to 600 MPa and then increased at 700 MPa pressure treatment. Fourier transform infrared spectroscopy (FT-IR) revealed that the conformational structure were changed from helices, sheets, turns, and aggregated strand to mostly intermolecular β-sheets or aggregated strands at pH 8 at 200 MPa but switched back to original structure at higher pressures.

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Sigma-Aldrich
Conalbumin from chicken egg white, BioReagent, suitable for cell culture
Sigma-Aldrich
Conalbumin from chicken egg white, Substantially iron-free
Sigma-Aldrich
Conalbumin from chicken egg white, Iron complex