Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing

被引:116
作者
Pearce, F. Grant
Mackintosh, Sarah H.
Gerrard, Juliet A.
机构
[1] Univ Canterbury, Sch Biol Sci, Christchurch 8020, New Zealand
[2] New Zealand Inst Crop & Food Res Ltd, Christchurch, New Zealand
关键词
ovalbumin; bovine serum albumin; amyloid fibril formation; heat denaturation;
D O I
10.1021/jf062154p
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Protein aggregation is important in food processing, and this work investigated the aggregation of food proteins as a source of amyloid fibrils for use in bionanotechnology. Both purified and crude mixtures of albumin proteins were denatured by heat, which caused aggregation to occur. Protein denaturation was measured by using circular dichroism spectrometry and by following thioflavin T fluorescence, which is widely used as a diagnostic test for amyloid formation. There was a good correlation between the increase in thioflavin T fluorescence and loss of helical structure as the temperature was increased. Formation of thioflavin T fluorescence was dependent on temperature, but less dependent on salt and protein concentration. X-ray fiber diffraction patterns of denatured bovine serum albumin suggested that the protein had a similar cross-beta structure to that of amyloid fibrils. These results are consistent with the aggregates seen during food processing, being amyloid-like in nature.
引用
收藏
页码:318 / 322
页数:5
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