Thermally induced aggregates in mixtures of α-lactalbumin with ovalbumins from different avian species

被引:18
|
作者
Sun, YX [1 ]
Hayakawa, S [1 ]
机构
[1] Kagawa Univ, Dept Biochem & Food Sci, Kagawa 7610795, Japan
关键词
avian; aggregation; gelation; heating; alpha-lactalbumin; ovalbumin; disulfide bond; sulfhydryl group;
D O I
10.1021/jf001086i
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Interactions between a-lactalbumin (alpha -La) and ovalbumin (OVA) in mixed systems (1:1 ratios; 2, 4, and 8% w/w total protein, respectively) heated at pH 7 and 80 degreesC for 15 min were studied using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), gel filtration chromatography (GFC), and competitive enzyme-linked immunosorbent assay (ELISA). Although a-La alone did not form aggregates upon heating, it formed large aggregates when heated with OVA. The aggregated molecules eluted at the void volume had a molecular mass > 300 kDa. The aggregation process was quantitatively affected by different avian OVAs from five species, possessing different numbers of free sulfhydryl groups. The amount of aggregates (M-w > 300 kDa) increased in proportion to total protein concentration, and the amount of intermediate components (M-w < 300 kDa) and monomeric OVA and alpha -La also changed, correlating with total protein concentration during heating. The results also indicated that the aggregates and intermediates, which contained dimeric and trimeric alpha -La, were mainly formed by the intermolecular disulfide bonds. The different interactions observed in several avian OVAs may explain heat-induced gelation of various avian OVAs as well as the enhancement of heat-induced gelation of OVA by alpha -La.
引用
收藏
页码:2511 / 2517
页数:7
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