title: Effect of high pressure treatment on ovotransferrin.
abstract: 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.
authors.affiliation: Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Canada, T6G 2P5.
authors.forename: Alexandra
authors.initials: A
authors.lastname: Acero-Lopez
authors.forename: Aman
authors.initials: A
authors.lastname: Ullah
authors.forename: Marina
authors.initials: M
authors.lastname: Offengenden
authors.forename: Stephanie
authors.initials: S
authors.lastname: Jung
authors.forename: Jianping
authors.initials: J
authors.lastname: Wu
mesh_terms: D002152:Calorimetry, Differential Scanning; D003207:Conalbumin / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011312:Pressure; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D003207:Conalbumin