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- W2007183779 abstract "Derivatives of β-lactoglobulin (β-LG) with isoelectric points (pIs) >7 enhanced the foaming of acidic proteins at pH 7. However, only basic proteins with pis >9.0 were capable of promoting foaming effectively in the presence of lipid. A derivative of mean pI 9.9 was particularly effective. Enzymic hydrolysis of clupeine (pI = 12; mol. wt = 4000) beyond a certain point caused a sudden reduction in foam-enhancing power, which coincided with a loss in the ability to form visible complexes (turbidity). Foam-enhancing properties of hydrolysed clupeine samples appeared to depend on their content of intact (enzyme-resistant) clupeine." @default.
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- W2007183779 date "1987-04-01" @default.
- W2007183779 modified "2023-09-26" @default.
- W2007183779 title "Charge and structural requirements of basic proteins for foam enhancement" @default.
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- W2007183779 doi "https://doi.org/10.1016/s0268-005x(87)80006-1" @default.
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