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• W2034891903 abstract "Limited proteolysis of β-lactoglobulin and β-casein by pepsin was performed in the presence of varying concentrations of ethanol. β-Lactoglobulin started to be cleaved by pepsin only in ethanol concentrations greater than 20%, when its secondary structure began to change. In 25% ethanol, the rate of hydrolysis of β-lactoglobulin was slow (40% remained intact after 40 h of hydrolysis) and many short and hydrophilic peptides were observed. The rate of hydrolysis of β-lactoglobulin reached its maximum in 30 and 35% ethanol (80% of β-lactoglobulin was hydrolysed after 10 h), and a mixed population of hydrophilic and hydrophobic peptides of different lengths was observed. Large hydrophobic peptides appeared first, then some shorter products. The rate of hydrolysis of β-lactoglobulin decreased at ethanol concentrations equal to or higher than 40%, when only a few long, hydrophobic peptides were produced. As seen by circular dichroism, the addition of ethanol to β-casein induced α-helix formation and reduced the rate of casein hydrolysis without changing the peptide profile. The only exception was the yield of a single peptide (Pro81 − Met93)." @default.
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• W2034891903 date "1995-01-01" @default.
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• W2034891903 title "Proteolysis of β-lactoglobulin and β-casein by pepsin in ethanolic media" @default.
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• W2034891903 doi "https://doi.org/10.1016/0958-6946(94)p1595-5" @default.
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