Abstract：
:β-Lactoglobulin (β-LG) is the major constituent of whey food, which has been shown to interact with a wide range of aroma compounds. In the present work, a model aroma compound, β-ionone, is used to investigate the influence of aroma compounds on the urea-induced unfolding of β-LG at pH 7.0. β-Ionone is observed to enhance the stability of β-LG at pH 7.0. Moreover, the amyloid fibrils are observed when β-LG at pH 7.0 is incubated for 12-20 days at 37 °C in the presence of 3-5M urea. However, the formation of amyloid fibrils is inhibited when β-ionone is added into the samples and the inhibitory effects follow a concentration-dependent fashion. There is a clear correlation between Cm and lag time. The correlation demonstrates that protein stability affects the amyloid fibril formation of β-LG. The results highlight the critical role of protein stability and provide an approach to prevent the formation of amyloid fibrils in vitro.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Ma B,You X,Lu Fdoi
10.1016/j.ijbiomac.2013.12.003subject
Has Abstractpub_date
2014-03-01 00:00:00pages
162-7eissn
0141-8130issn
1879-0003pii
S0141-8130(13)00652-1journal_volume
64pub_type
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