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- W2035315302 abstract "Proteins tend to form inactive aggregates at high temperatures. We show that polyamines, which have a relatively simple structure as oligoamids, effectively prevent thermal inactivation and aggregation of hen egg lysozyme. In the presence of additives, including arginine and guanidine (100 m m ), more than 30% of 0.2 mg·mL −1 lysozyme in sodium phosphate buffer (pH 6.5) formed insoluble aggregates by heat treatment (98 °C for 30 min). However, in the presence of 50 m m spermine or spermidine, no aggregates were observed after the same heat treatment. The residual activity of lysozyme after this heat treatment was very low (< 5%), even in the presence of 100 m m arginine and guanidine, while it was maintained at ≈ 50% in the presence of 100 m m spermine and spermidine. These results imply that polyamines are new candidates as molecular additives for preventing the thermal aggregation and inactivation of heat‐labile proteins." @default.
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- W2035315302 date "2003-10-19" @default.
- W2035315302 modified "2023-10-17" @default.
- W2035315302 title "Prevention of thermal inactivation and aggregation of lysozyme by polyamines" @default.
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- W2035315302 doi "https://doi.org/10.1046/j.1432-1033.2003.03850.x" @default.
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