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- W2057072016 abstract "The pH 4.6-soluble fraction of the peptic hydrolyzate of as 1-casein contained the 23 N-terminal residues, αsl-CN(fl-23), as a major pep-tide. Reversed-phase HPLC indicated that small amounts of other peptides such as αsl-CN(f154-199) were also contained in this fraction. By removing of these peptides, the emulsifying activity (EA) of the αsl-CN(fl-23) fraction was markedly decreased. However, when the removed peptide fraction was added to the purified αsl-CN(fl-23), the EA was increased. Some synergistic effect in the emulsification seemed to exist between αsl-CN(fl-23) and the other peptides. Although the purified αsl-CN(fl-23) had low EA values at neutral pH levels, it showed high emulsifying and surface activities in the acidic pH region." @default.
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- W2057072016 date "1986-09-01" @default.
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- W2057072016 title "Functional Properties of a Peptide of 23 Residues Purified from the Peptic Hydrolyzate of asl-CASEIN: Changes in the Emulsifying Activity During Purification of the Peptide" @default.
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- W2057072016 doi "https://doi.org/10.1111/j.1365-2621.1986.tb13097.x" @default.
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