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- W2346346068 abstract "Prior published papers has been reanalyzed in this retrospective study of β-lactoglobulin (β-LG) coerced into forming amyloids through assays using both light scattering and Thioflavin T (ThT) fluorescence. The published datasets were extracted and analyzed by a sigmoidal time-dependent model, which yields two time constants which allow comparison between various concentration levels of protein in solution, denaturing temperature, some other additives and the presence of mechanical agitation, however that was accomplished. Shorter aggregation times are observed with increased protein concentration in solution and increased denaturing temperature. The presence of agitation seems to have a large influence and future efforts should be clear to identify the type of agitation if standards are to be developed. Finally comparing scattering and ThT fluorescence, as indicators, it appears that scattering occurs at an earlier time point relative to ThT fluorescence linked with β sheet formation." @default.
- W2346346068 created "2016-06-24" @default.
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- W2346346068 date "2016-11-01" @default.
- W2346346068 modified "2023-09-22" @default.
- W2346346068 title "A meta analysis of β-lactoglobulin aggregation kinetics comparing temperature, concentration, and chemistry as modulating influences" @default.
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- W2346346068 doi "https://doi.org/10.1016/j.jfoodeng.2016.05.004" @default.
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