FOOD SCIENCE
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DENG Guogang, LI Canpeng*
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Published:
Abstract: In this study, the effects of phosphorylated ovalbumin (PP-OVA) on heat-induced aggregation of native ovalbumin (N-OVA) were investigated. Results showed that PP-OVA effectively suppressed N-OVA aggregation, and the inhibited ability is little weakened when the ionic strength ranged from 10 to 100 mmol/L. Dynamic light scattering analysis showed that the size of the formed N-OVA aggregates decreased in the presence of PP-OVA. Transmission electron micrographs further showed that the N-OVA/PP-OVA mixture exhibited a more uniform size distribution than N-OVA alone. After heat treatment solution of N-OVA, the ζ-potential increased with PP-OVA increased, suggesting that the system became more stable. The result of native-PAGE suggested that the N-OVA/PP-OVA aggregates possess a well-solubility and homogeneity. These results indicate that PP-OVA exhibits a chaperone-like activity under heating, and provide an insight into the possible mechanism through which PP-OVA stabilizes proteins to resist heat-induced N-OVA aggregation.
CLC Number:
Q518.4
DENG Guogang, LI Canpeng. Heat-Induced Aggregation Inhibition Properties of Phosphorylated Ovalbumin through Its Molecular Chaperone-like Properties[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201705011.
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URL: https://www.spkx.net.cn/EN/10.7506/spkx1002-6630-201705011
https://www.spkx.net.cn/EN/Y2017/V38/I5/66