Effect of high pressure treatment on ovotransferrin

被引:51
作者
Acero-Lopez, Alexandra [1 ]
Ullah, Aman [1 ]
Offengenden, Marina [1 ]
Jung, Stephanie [2 ]
Wu, Jianping [1 ]
机构
[1] Univ Alberta, Dept Agr Food & Nutr Sci, Edmonton, AB T6G 2P5, Canada
[2] Iowa State Univ, Dept Food Sci & Human Nutr, Ctr Crops Utilizat Res, Ames, IA 50011 USA
关键词
Ovotransferrin; High pressure; pH; Physicochemical properties; Aggregation; EGG-WHITE PROTEINS; ANTIVIRAL ACTIVITY; FOOD; FLUORESCENCE; SPECTROSCOPY; STATE; PASTEURIZATION; TEMPERATURE; PEPTIDES; ANIONS;
D O I
10.1016/j.foodchem.2012.07.071
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
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 beta-sheets or aggregated strands at pH 8 at 200 MPa but switched back to original structure at higher pressures. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2245 / 2252
页数:8
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